Keratin intermediate filament chains in the European common wall lizard (Podarcis muralis) and a potential keratin filament crosslinker

•Sequences of 28 Type I and II KIF chains in common wall lizard.•Type I and II genes lie in clusters on chromosomes 13 and 2 respectively.•Heads and tails of KIF chains contain many sequences repeats.•H1 subdomain (Type II) is conserved and has a role in assembly.•Potential KIF crosslinker with tand...

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Published inJournal of structural biology Vol. 213; no. 4; p. 107793
Main Authors Parry, David A.D., Winter, David J.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.12.2021
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Abstract •Sequences of 28 Type I and II KIF chains in common wall lizard.•Type I and II genes lie in clusters on chromosomes 13 and 2 respectively.•Heads and tails of KIF chains contain many sequences repeats.•H1 subdomain (Type II) is conserved and has a role in assembly.•Potential KIF crosslinker with tandem repeats in tail is identified. On the basis of sequence homology with mammalian α-keratins, and on the criteria that the coiled-coil segments and central linker in the rod domain of these molecules must have conserved lengths if they are to assemble into viable intermediate filaments, a total of 28 Type I and Type II keratin intermediate filament chains (KIF) have been identified from the genome of the European common wall lizard (Podarcis muralis). Using the same criteria this number may be compared to 33 found here in the green anole lizard (Anole carolinensis) and 25 in the tuatara (Sphenodon punctatus). The Type I and Type II KIF genes in the wall lizard fall in clusters on chromosomes 13 and 2 respectively. Although some differences occur in the terminal domains in the KIF chains of the two lizards and tuatara, the similarities between key indicator residues – cysteine, glycine and proline – are significant. The terminal domains of the KIF chains in the wall lizard also contain sequence repeats commonly based on glycine and large apolar residues and would permit the fine tuning of physical properties when incorporated within the intermediate filaments. The H1 domain in the Type II chain is conserved across the lizards, tuatara and mammals, and has been related to its role in assembly at the 2–4 molecule level. A KIF-like chain (K80) with an extensive tail domain comprised of multiple tandem repeats has been identified as having a potential filament-crosslinking role.
AbstractList •Sequences of 28 Type I and II KIF chains in common wall lizard.•Type I and II genes lie in clusters on chromosomes 13 and 2 respectively.•Heads and tails of KIF chains contain many sequences repeats.•H1 subdomain (Type II) is conserved and has a role in assembly.•Potential KIF crosslinker with tandem repeats in tail is identified. On the basis of sequence homology with mammalian α-keratins, and on the criteria that the coiled-coil segments and central linker in the rod domain of these molecules must have conserved lengths if they are to assemble into viable intermediate filaments, a total of 28 Type I and Type II keratin intermediate filament chains (KIF) have been identified from the genome of the European common wall lizard (Podarcis muralis). Using the same criteria this number may be compared to 33 found here in the green anole lizard (Anole carolinensis) and 25 in the tuatara (Sphenodon punctatus). The Type I and Type II KIF genes in the wall lizard fall in clusters on chromosomes 13 and 2 respectively. Although some differences occur in the terminal domains in the KIF chains of the two lizards and tuatara, the similarities between key indicator residues – cysteine, glycine and proline – are significant. The terminal domains of the KIF chains in the wall lizard also contain sequence repeats commonly based on glycine and large apolar residues and would permit the fine tuning of physical properties when incorporated within the intermediate filaments. The H1 domain in the Type II chain is conserved across the lizards, tuatara and mammals, and has been related to its role in assembly at the 2–4 molecule level. A KIF-like chain (K80) with an extensive tail domain comprised of multiple tandem repeats has been identified as having a potential filament-crosslinking role.
On the basis of sequence homology with mammalian α-keratins, and on the criteria that the coiled-coil segments and central linker in the rod domain of these molecules must have conserved lengths if they are to assemble into viable intermediate filaments, a total of 28 Type I and Type II keratin intermediate filament chains (KIF) have been identified from the genome of the European common wall lizard (Podarcis muralis). Using the same criteria this number may be compared to 33 found here in the green anole lizard (Anole carolinensis) and 25 in the tuatara (Sphenodon punctatus). The Type I and Type II KIF genes in the wall lizard fall in clusters on chromosomes 13 and 2 respectively. Although some differences occur in the terminal domains in the KIF chains of the two lizards and tuatara, the similarities between key indicator residues - cysteine, glycine and proline - are significant. The terminal domains of the KIF chains in the wall lizard also contain sequence repeats commonly based on glycine and large apolar residues and would permit the fine tuning of physical properties when incorporated within the intermediate filaments. The H1 domain in the Type II chain is conserved across the lizards, tuatara and mammals, and has been related to its role in assembly at the 2-4 molecule level. A KIF-like chain (K80) with an extensive tail domain comprised of multiple tandem repeats has been identified as having a potential filament-crosslinking role.
ArticleNumber 107793
Author Parry, David A.D.
Winter, David J.
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Cites_doi 10.1016/0022-2836(77)90153-X
10.1016/S0021-9258(19)38954-9
10.1146/annurev.biochem.73.011303.073823
10.1002/jez.b.21241
10.1006/jmbi.1993.1161
10.1016/S0021-9258(18)53855-2
10.1083/jcb.111.1.153
10.1007/s11837-012-0302-8
10.2108/zsj.23.801
10.1126/science.aan6398
10.1002/jez.b.21306
10.1006/jsbi.2002.4438
10.1016/j.jsb.2020.107599
10.1083/jcb.110.4.1199
10.1186/s12862-015-0360-y
10.1186/1471-2148-10-148
10.1007/978-3-319-49674-0_8
10.1021/pr301036k
10.1093/nar/gkh340
10.1016/S0022-2836(05)80101-9
10.1017/S0033583500003516
10.1242/jcs.089516
10.1007/978-981-10-8195-8_6
10.1078/0171-9335-00354
10.1093/bioinformatics/btp033
10.1038/nature10390
10.1093/molbev/msr269
10.1073/pnas.0805154105
10.1016/j.jsb.2017.09.003
10.1016/S0006-291X(85)80045-0
10.1074/jbc.274.14.9881
10.1016/0141-8130(83)90040-5
10.1002/jez.b.22840
10.1093/molbev/msz279
10.1016/S0065-3233(06)73001-7
10.1016/bs.ircmb.2016.06.005
10.1038/s41586-020-2561-9
10.1021/bi00089a021
10.3390/genes12040591
10.1016/j.jsb.2015.10.017
10.1016/j.pmatsci.2015.06.001
10.1083/jcb.151.7.1459
10.1002/jez.b.22514
10.1016/j.jsb.2021.107706
10.1073/pnas.1820320116
10.1186/s12862-014-0249-1
10.1016/j.ejcb.2005.01.007
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Issue 4
Keywords Epidermal appendages
Lizard keratin
Sequence repeats
Keratin intermediate filament chains
Filament crosslinker
Language English
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References Dalla Valle, Nardi, Gelmi, Toni, Emera, Alibardi (b0040) 2009; 312B
Edgar (b0055) 2004; 32
McKittrick, Chen, Bodde, Yang, Novitskaya, Meyers (b0140) 2012; 64
Coulombe, Fuchs (b0030) 1990; 111
Fraser, R.D.B., Parry, D.A.D. 2018. Structural hierarchy of trichocyte keratin intermediate filaments. In: The Hair Fibre: Proteins, Structure and Development (eds J. Plowman, D. Harland and S. Deb-Choudhury) Adv. Exp. Med. Biol. 1054, pp 57-70, Springer.
Rice, Winters, Durbin-Johnson, Rocke (b0180) 2013; 12
Hatzfeld, Weber (b0110) 1990; 110
Dalla Valle, Nardi, Bonazza, Zuccal, Emera, Alibardi (b0045) 2010; 314B
Hughes, M.P., Sawaya, M.R., Boyer, D.R., Goldschmidt, L., Rodriguez, J.A., Cascio, D., Chong, L., Gonen, T., Eisenberg, D.S. Atomic structures of low-complexity protein segments reveal kinked ß-sheets that assemble networks. Science 359, 698-701.
Greenwold, Sawyer (b0100) 2013; 320B
Kajava, A.V., Squire, J.M., Parry, D.A.D. 2006. ß-structures in fibrous proteins. Adv. Pro. Chem. (eds Parry, D.A.D., Squire, J.M.) 73, 1-15.
Strasser, Mlitz, Hermann, Tschachler, Eckhart (b0215) 2015; 15
Waterhouse, Procter, Martin, Clamp, Barton (b0240) 2009; 25
Fraser, MacRae, Rogers (b0085) 1972
Alibardi, Toni (b0015) 2006; 23
Alföldi, Di Palma, Grabherr, Williams, Kong, Mauceli, Russell, Lowe, Glor, Jaffe, Ray, Boissinot, Shedlock, Botka, Castoe, Colbourne, Fujita, Moreno, ten Hallers, Haussler, Heger, Heiman, Janes, Johnson, de Jong, Koriabine, Lara, Novick, Organ, Peach, Poe, Pollock, de Queiroz, Sanger, Searle, Smith, Smith, Swofford, Turner-Maier, Wade, Young, Zadissa, Edwards, Glenn, Schneider, Losos, Lander, Breen, Ponting, Lindblad-Toh (b0005) 2011; 477
Alibardi (b0010) 2016; 327
Strnad, Usachov, Debes, Grater, Parry, Omary (b0220) 2011; 124
Parry, D.A.D., Winter, D.J. 2021. Keratin intermediate filament chains in tuatara (Sphenodon punctatus): a comparison of tuatara and human sequences. J. Struct. Biol. 213, 107706.
Vandebergh, Bossuyt (b0225) 2012; 29
Parry (b0145) 2020; 212
Ehrlich, Lachner, Hermann, Tschachler, Eckhart (b0060) 2020; 37
Steinert (b0190) 1990; 265
Holthaus, Eckhart, Dalla Valle, Alibardi (b0125) 2018; 330
Yates, Achuthan, Akanni, Allen, Allen, Alvarez-Jarreta, Amode, Armean, Azov, Bennett, Bhai, Billis, Boddu, Marugan, Cummins, Davidson, Dodiya, Fatima, Gall, Giron, Gil, Grego, Haggerty, Haskell, Hourlier, Izuogu, Janacek, Juettermann, Kay, Lavidas, Le, Lemos, Martinez, Maurel, McDowell, McMahon, Mohanan, Moore, Nuhn, Oheh, Parker, Parton, Patricio, Sakthivel, Salam, Schmitt, Schuilenburg, Sheppard, Sycheva, Szuba, Taylor, Thormann, Threadgold, Vullo, Walts, Winterbottom, Zadissa, Chakiachvili, Flint, Frankish, Hunt, Ilsley, Kostadima, Langridge, Loveland, Martin, Morales, Mudge, Muffato, Perry, Ruffier, Trevanion, Cunningham, Howe, Zerbino, Flicek (b0250) 2020; 48
Andrade, P., Pinho, C., Perez i de Lanuza, G., Afonso, S., Brejcha, J., Rubin, C-J., Wallerman, O., Pereira, P., Sabatino, S.J., Bellati, A., Pellitteri-Rosa, D., Bosakova, Z., Bunikis, I., Carretero, M.A., Feiner, N., Marsik, P., Pauperio, F., Salvi, D., Soler, L., While, G.M., Uller, T., Font, E., Andersson, L., Carneiro, M. 2019. Regulatory changes in pterin and carotenoid genes underlie balanced color polymorphism in the wall lizard. Proc. Natl. Acad. Sci. USA, 116, 5633-5642.
Eckhart, Dalla Valle, Jaeger, Ballaun, Szabo, Nardi, Buchberger, Hermann, Alibardi, Tschachler (b0050) 2008; 105
Steinert, Marekov, Parry (b0205) 1993; 32
Bullough, Tulloch (b0025) 1990; 215
Parry, Steinert (b0160) 1999; 32
Zimek, Weber (b0255) 2005; 84
Smith, Strelkov, Burkhard, Aebi, Parry (b0185) 2002; 137
Gemmell, Rutherford, Prost, Tollis, Winter, Macey, Adelson, Suh, Bertozzi, Grau, Organ, Gardner, Muffato, Patricio, Billis, Martin, Flicek, Petersen, Kang, Michalak, Buckley, Wilson, Cheng, Miller, Schott, Jordan, Newcomb, Arroyo, Valenzuela, Hore, Renart, Peona, Peart, Warmuth, Zeng, Kortschak, Raison, Zapata, Wu, Santesmasses, Mariotti, Guigo, Rupp, Twort, Dussex, Taylor, Abe, Paterson, Mulcahy, Gonzalez, Barbieri, DeMeo, Pabinger, Ryder, Edwards, Salzberg, Mickelson, Nelson, Stone, Ngatiwai Trust Board (b0090) 2020; 584
Parry, Steinert (b0155) 1995
Steinert, Chou, Prahlad, Parry, Marekov, Wu, Jang, Goldman (b0210) 1999; 274
Greenwold, Sawyer (b0095) 2010; 10
Parry, Steven, Steinert (b0175) 1985; 127
Fraser, Parry (b0075) 2017; 200
Fraser, R.D.B., Parry, D.A.D. 2017a. Filamentous structure of hard β-keratin in the epidermal appendages of birds and reptiles. In: Subcellular Biochemistry: Fibrous Proteins: Structures and Mechanisms (eds Parry, D.A.D. and Squire, J.M.) vol. 82, pp 231-252, Springer International Publishing Switzerland. doi: 10.1007/978-3-319-49674-0_8.
Greenwold, Bao, Jarvis, Hu, Li, Gilbert, Zhang, Sawyer (b0105) 2014; 14
Wu, Ng, Yan, Lai, Chen, Lai, Wu, Chen, Luo, Widelitz, Li, Chuong (b0245) 2015; 122
Wang, Parry, Jones, Idler, Marekov, Steinert (b0235) 2000; 151
Herrmann, Aebi (b0115) 2004; 73
Fraser, Parry (b0065) 2015; 192
Parry, Crewther, Fraser, MacRae (b0170) 1977; 113
Steinert, Parry (b0195) 1993; 268
Hesse, Zimek, Weber, Magin (b0120) 2004; 83
Steinert, Marekov, Fraser, Parry (b0200) 1993; 230
Crewther, Dowling, Steinert, Parry (b0035) 1983; 5
Parry (b0150) 2021; 12
Wang, Yang, McKittrick, Meyers (b0230) 2016; 76
Vandebergh (10.1016/j.jsb.2021.107793_b0225) 2012; 29
Yates (10.1016/j.jsb.2021.107793_b0250) 2020; 48
McKittrick (10.1016/j.jsb.2021.107793_b0140) 2012; 64
Crewther (10.1016/j.jsb.2021.107793_b0035) 1983; 5
Dalla Valle (10.1016/j.jsb.2021.107793_b0040) 2009; 312B
10.1016/j.jsb.2021.107793_b0080
Greenwold (10.1016/j.jsb.2021.107793_b0105) 2014; 14
Alibardi (10.1016/j.jsb.2021.107793_b0010) 2016; 327
Wang (10.1016/j.jsb.2021.107793_b0235) 2000; 151
10.1016/j.jsb.2021.107793_b0165
Wang (10.1016/j.jsb.2021.107793_b0230) 2016; 76
Dalla Valle (10.1016/j.jsb.2021.107793_b0045) 2010; 314B
Eckhart (10.1016/j.jsb.2021.107793_b0050) 2008; 105
Herrmann (10.1016/j.jsb.2021.107793_b0115) 2004; 73
Parry (10.1016/j.jsb.2021.107793_b0150) 2021; 12
Gemmell (10.1016/j.jsb.2021.107793_b0090) 2020; 584
Parry (10.1016/j.jsb.2021.107793_b0145) 2020; 212
Strasser (10.1016/j.jsb.2021.107793_b0215) 2015; 15
Holthaus (10.1016/j.jsb.2021.107793_b0125) 2018; 330
10.1016/j.jsb.2021.107793_b0070
Hatzfeld (10.1016/j.jsb.2021.107793_b0110) 1990; 110
Parry (10.1016/j.jsb.2021.107793_b0175) 1985; 127
Steinert (10.1016/j.jsb.2021.107793_b0195) 1993; 268
Coulombe (10.1016/j.jsb.2021.107793_b0030) 1990; 111
Rice (10.1016/j.jsb.2021.107793_b0180) 2013; 12
Greenwold (10.1016/j.jsb.2021.107793_b0100) 2013; 320B
Ehrlich (10.1016/j.jsb.2021.107793_b0060) 2020; 37
Steinert (10.1016/j.jsb.2021.107793_b0205) 1993; 32
Steinert (10.1016/j.jsb.2021.107793_b0200) 1993; 230
Alibardi (10.1016/j.jsb.2021.107793_b0015) 2006; 23
Parry (10.1016/j.jsb.2021.107793_b0170) 1977; 113
Steinert (10.1016/j.jsb.2021.107793_b0210) 1999; 274
Wu (10.1016/j.jsb.2021.107793_b0245) 2015; 122
Fraser (10.1016/j.jsb.2021.107793_b0075) 2017; 200
Zimek (10.1016/j.jsb.2021.107793_b0255) 2005; 84
Steinert (10.1016/j.jsb.2021.107793_b0190) 1990; 265
Smith (10.1016/j.jsb.2021.107793_b0185) 2002; 137
10.1016/j.jsb.2021.107793_b0020
Parry (10.1016/j.jsb.2021.107793_b0160) 1999; 32
Strnad (10.1016/j.jsb.2021.107793_b0220) 2011; 124
Waterhouse (10.1016/j.jsb.2021.107793_b0240) 2009; 25
Greenwold (10.1016/j.jsb.2021.107793_b0095) 2010; 10
Parry (10.1016/j.jsb.2021.107793_b0155) 1995
10.1016/j.jsb.2021.107793_b0130
10.1016/j.jsb.2021.107793_b0135
Fraser (10.1016/j.jsb.2021.107793_b0065) 2015; 192
Alföldi (10.1016/j.jsb.2021.107793_b0005) 2011; 477
Fraser (10.1016/j.jsb.2021.107793_b0085) 1972
Edgar (10.1016/j.jsb.2021.107793_b0055) 2004; 32
Bullough (10.1016/j.jsb.2021.107793_b0025) 1990; 215
Hesse (10.1016/j.jsb.2021.107793_b0120) 2004; 83
References_xml – volume: 12
  start-page: 771
  year: 2013
  end-page: 776
  ident: b0180
  article-title: Chicken corneocyte cross-linked proteome
  publication-title: J. Proteome Res.
  contributor:
    fullname: Rocke
– volume: 312B
  start-page: 42
  year: 2009
  end-page: 57
  ident: b0040
  article-title: β-keratins of the crocodilian epidermis: composition, structure, and phylogenetic relationships
  publication-title: J. Exp. Biol. (Mol. Dev. Evol.)
  contributor:
    fullname: Alibardi
– volume: 137
  start-page: 128
  year: 2002
  end-page: 145
  ident: b0185
  article-title: Sequence comparisons of intermediate filament chains: evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1
  publication-title: J. Struct. Biol.
  contributor:
    fullname: Parry
– start-page: 1
  year: 1995
  end-page: 183
  ident: b0155
  article-title: Intermediate filament structure
  contributor:
    fullname: Steinert
– volume: 83
  start-page: 19
  year: 2004
  end-page: 26
  ident: b0120
  article-title: Comprehensive analysis of keratin gene clusters in humans and rodents
  publication-title: Eur. J. Cell Biol.
  contributor:
    fullname: Magin
– year: 1972
  ident: b0085
  article-title: Keratins – their composition, structure and biosynthesis
  contributor:
    fullname: Rogers
– volume: 215
  start-page: 161
  year: 1990
  end-page: 173
  ident: b0025
  article-title: High-resolution spot-scan electron microscopy of microcrystals of an α-helical coiled-coil protein
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Tulloch
– volume: 327
  start-page: 263
  year: 2016
  end-page: 319
  ident: b0010
  article-title: The process of cornification evolved from the initial keratinization in the epidermis and epidermal derivatives of vertebrates: a new synthesis and the case of sauropsids
  publication-title: Int. Rev. Cell Mol. Biol.
  contributor:
    fullname: Alibardi
– volume: 274
  start-page: 9881
  year: 1999
  end-page: 9890
  ident: b0210
  article-title: A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a type VI intermediate filament protein: limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV α-internexin
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Goldman
– volume: 76
  start-page: 229
  year: 2016
  end-page: 318
  ident: b0230
  article-title: Keratin: structure, mechanical properties, occurrence in biological organisms and efforts in bioinspiration
  publication-title: Progr. Mater. Sci.
  contributor:
    fullname: Meyers
– volume: 37
  start-page: 982
  year: 2020
  end-page: 993
  ident: b0060
  article-title: Convergent evolution of cysteine-rich keratins in hard skin appendages of terrestrial vertebrates
  publication-title: Mol. Biol. Evol.
  contributor:
    fullname: Eckhart
– volume: 48
  start-page: D682
  year: 2020
  end-page: D688
  ident: b0250
  article-title: Ensembl 2020
  publication-title: Nucl. Acids Res.
  contributor:
    fullname: Flicek
– volume: 265
  start-page: 8766
  year: 1990
  end-page: 8774
  ident: b0190
  article-title: The two-chain coiled-coil molecule of native epidermal keratin intermediate filaments is a type I-type II heterodimer
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Steinert
– volume: 584
  start-page: 403
  year: 2020
  end-page: 409
  ident: b0090
  article-title: The tuatara genome reveals ancient features of amniote evolution
  publication-title: Nature
  contributor:
    fullname: Ngatiwai Trust Board
– volume: 330
  start-page: 438
  year: 2018
  end-page: 453
  ident: b0125
  article-title: Review: Evolution and diversification of corneous beta-proteins, the characteristic epidermal proteins of reptiles and birds
  publication-title: J. Exp. Zool. (Mol. Dev. Evol.)
  contributor:
    fullname: Alibardi
– volume: 84
  start-page: 623
  year: 2005
  end-page: 635
  ident: b0255
  article-title: Terrestrial vertebrates have two keratin gene clusters: striking differences in teleost fish
  publication-title: Eur. J. Cell Biol.
  contributor:
    fullname: Weber
– volume: 105
  start-page: 18419
  year: 2008
  end-page: 18423
  ident: b0050
  article-title: Identification of reptilian genes encoding hair keratin-like proteins suggests a new scenario for the evolutionary origin of hair
  publication-title: Proc. Natl. Acad. Sci. USA
  contributor:
    fullname: Tschachler
– volume: 29
  start-page: 995
  year: 2012
  end-page: 1004
  ident: b0225
  article-title: Radiation and functional diversification of alpha keratins during early vertebrate evolution
  publication-title: Mol. Biol. Evol.
  contributor:
    fullname: Bossuyt
– volume: 320B
  start-page: 393
  year: 2013
  end-page: 405
  ident: b0100
  article-title: Molecular evolution and expression of archosaurian β-keratins and the origin of feather β-keratins
  publication-title: J. Exp. Zool. Mol. Dev. Evol.
  contributor:
    fullname: Sawyer
– volume: 10
  start-page: 148
  year: 2010
  ident: b0095
  article-title: Genomic organization and molecular phylogenies of the beta (β) keratin multigene family in the chicken (
  publication-title: BMC Evol. Biol.
  contributor:
    fullname: Sawyer
– volume: 23
  start-page: 801
  year: 2006
  end-page: 807
  ident: b0015
  article-title: Distribution and characterization of keratins in the epidermis of the tuatara (
  publication-title: Zool. Sci.
  contributor:
    fullname: Toni
– volume: 5
  start-page: 267
  year: 1983
  end-page: 274
  ident: b0035
  article-title: Structure of intermediate filaments
  publication-title: Int. J. Biol. Macromol.
  contributor:
    fullname: Parry
– volume: 151
  start-page: 1459
  year: 2000
  end-page: 1468
  ident: b0235
  article-title: In vitro assembly and structure of trichocyte keratin intermediate filaments: a novel role for stabilization by disulfide bonding
  publication-title: J. Cell Biol.
  contributor:
    fullname: Steinert
– volume: 14
  start-page: 249
  year: 2014
  ident: b0105
  article-title: Dynamic evolution of the alpha (α) and beta (β) keratins has accompanied integument diversification and the adaption of birds into novel lifestyles
  publication-title: BMC Evol. Biol.
  contributor:
    fullname: Sawyer
– volume: 124
  start-page: 4221
  year: 2011
  end-page: 4232
  ident: b0220
  article-title: Unique amino acid signatures that are evolutionarily conserved distinguish simple-type, epidermal and hair keratins
  publication-title: J. Cell Sci.
  contributor:
    fullname: Omary
– volume: 32
  start-page: 99
  year: 1999
  end-page: 187
  ident: b0160
  article-title: Intermediate Filaments: Molecular Architecture, Assembly, Dynamics and Polymorphism
  publication-title: Q. Rev. Biophys.
  contributor:
    fullname: Steinert
– volume: 268
  start-page: 2878
  year: 1993
  end-page: 2887
  ident: b0195
  article-title: The conserved H1 domain of the type II keratin 1 chain plays an essential role in the alignment of nearest-neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two- to four-molecule level of structure
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Parry
– volume: 25
  start-page: 1189
  year: 2009
  end-page: 1191
  ident: b0240
  article-title: Jalview version 2 - a multiple sequence alignment editor and analysis workbench
  publication-title: Bioinformatics.
  contributor:
    fullname: Barton
– volume: 200
  start-page: 45
  year: 2017
  end-page: 53
  ident: b0075
  article-title: Intermediate filament structure in fully differentiated (oxidised) trichocyte keratin
  publication-title: J. Struct. Biol.
  contributor:
    fullname: Parry
– volume: 32
  start-page: 10046
  year: 1993
  end-page: 10056
  ident: b0205
  article-title: Conservation of the structure of keratin intermediate filaments: molecular mechanism by which different keratin molecules integrate into pre-existing keratin intermediate filaments during differentiation
  publication-title: Biochem.
  contributor:
    fullname: Parry
– volume: 212
  year: 2020
  ident: b0145
  article-title: Structure and topology of the linkers in the conserved lepidosaur β-keratin chain with four 34-residue repeats support an interfilament role for the central linker
  publication-title: J. Struct. Biol.
  contributor:
    fullname: Parry
– volume: 12
  start-page: 591
  year: 2021
  ident: b0150
  article-title: Structures of the β-keratin filaments and keratin intermediate filaments in the epidermal appendages of birds and reptiles (sauropsids)
  publication-title: Genes.
  contributor:
    fullname: Parry
– volume: 192
  start-page: 528
  year: 2015
  end-page: 538
  ident: b0065
  article-title: The molecular structure of the silk fibers from
  publication-title: J. Struct. Biol.
  contributor:
    fullname: Parry
– volume: 111
  start-page: 153
  year: 1990
  end-page: 169
  ident: b0030
  article-title: Elucidating the early stages of keratin filament assembly
  publication-title: J. Cell Biol.
  contributor:
    fullname: Fuchs
– volume: 477
  start-page: 587
  year: 2011
  end-page: 591
  ident: b0005
  article-title: The genome of the green anole lizard and a comparative analysis with birds and mammals
  publication-title: Nature
  contributor:
    fullname: Lindblad-Toh
– volume: 32
  start-page: 1792
  year: 2004
  end-page: 1797
  ident: b0055
  article-title: MUSCLE: multiple sequence alignment with high accuracy and high throughput
  publication-title: Nucl. Acids Res.
  contributor:
    fullname: Edgar
– volume: 15
  start-page: 82
  year: 2015
  ident: b0215
  article-title: Convergent evolution of cysteine-rich proteins in feathers and hair
  publication-title: BMC Evol. Biol.
  contributor:
    fullname: Eckhart
– volume: 314B
  start-page: 11
  year: 2010
  end-page: 32
  ident: b0045
  article-title: Forty keratin-associated beta-proteins (β-proteins) form the hard layers of scales, claws, adhesive pads in the green anole lizard
  publication-title: . J. Exp. Zool
  contributor:
    fullname: Alibardi
– volume: 113
  start-page: 449
  year: 1977
  end-page: 454
  ident: b0170
  article-title: Structure of α-keratin: structural implications of the amino acid sequences of the type I and type II chain segments
  publication-title: J. Mol. Biol.
  contributor:
    fullname: MacRae
– volume: 122
  start-page: E6770
  year: 2015
  end-page: E6779
  ident: b0245
  article-title: Topographical mapping of α- and β-keratins on developing chicken skin integument: functional interaction and evolutionary perspectives
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Chuong
– volume: 230
  start-page: 436
  year: 1993
  end-page: 452
  ident: b0200
  article-title: Keratin intermediate filament structure: crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Parry
– volume: 73
  start-page: 749
  year: 2004
  end-page: 789
  ident: b0115
  article-title: Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
  publication-title: Annu. Rev. Biochem.
  contributor:
    fullname: Aebi
– volume: 127
  start-page: 1012
  year: 1985
  end-page: 1018
  ident: b0175
  article-title: The coiled-coil molecules of intermediate filaments consist of two parallel chains in exact axial register
  publication-title: Biochem. Biophys. Res. Commun.
  contributor:
    fullname: Steinert
– volume: 110
  start-page: 1199
  year: 1990
  end-page: 1210
  ident: b0110
  article-title: The coiled-coil of in vitro assembled keratin filaments is a heterodimer of Type I and II keratin: use of site-specific mutagenesis and recombinant protein expression
  publication-title: J. Cell Biol.
  contributor:
    fullname: Weber
– volume: 64
  start-page: 449
  year: 2012
  end-page: 468
  ident: b0140
  article-title: The structure, function, and mechanical properties of keratin
  publication-title: JOM
  contributor:
    fullname: Meyers
– volume: 48
  start-page: D682
  issue: D1
  year: 2020
  ident: 10.1016/j.jsb.2021.107793_b0250
  article-title: Ensembl 2020
  publication-title: Nucl. Acids Res.
  contributor:
    fullname: Yates
– volume: 113
  start-page: 449
  year: 1977
  ident: 10.1016/j.jsb.2021.107793_b0170
  article-title: Structure of α-keratin: structural implications of the amino acid sequences of the type I and type II chain segments
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(77)90153-X
  contributor:
    fullname: Parry
– volume: 265
  start-page: 8766
  year: 1990
  ident: 10.1016/j.jsb.2021.107793_b0190
  article-title: The two-chain coiled-coil molecule of native epidermal keratin intermediate filaments is a type I-type II heterodimer
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)38954-9
  contributor:
    fullname: Steinert
– volume: 73
  start-page: 749
  year: 2004
  ident: 10.1016/j.jsb.2021.107793_b0115
  article-title: Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.73.011303.073823
  contributor:
    fullname: Herrmann
– volume: 312B
  start-page: 42
  year: 2009
  ident: 10.1016/j.jsb.2021.107793_b0040
  article-title: β-keratins of the crocodilian epidermis: composition, structure, and phylogenetic relationships
  publication-title: J. Exp. Biol. (Mol. Dev. Evol.)
  doi: 10.1002/jez.b.21241
  contributor:
    fullname: Dalla Valle
– volume: 230
  start-page: 436
  issue: 2
  year: 1993
  ident: 10.1016/j.jsb.2021.107793_b0200
  article-title: Keratin intermediate filament structure: crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1993.1161
  contributor:
    fullname: Steinert
– volume: 268
  start-page: 2878
  year: 1993
  ident: 10.1016/j.jsb.2021.107793_b0195
  article-title: The conserved H1 domain of the type II keratin 1 chain plays an essential role in the alignment of nearest-neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two- to four-molecule level of structure
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)53855-2
  contributor:
    fullname: Steinert
– volume: 111
  start-page: 153
  year: 1990
  ident: 10.1016/j.jsb.2021.107793_b0030
  article-title: Elucidating the early stages of keratin filament assembly
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.111.1.153
  contributor:
    fullname: Coulombe
– volume: 64
  start-page: 449
  year: 2012
  ident: 10.1016/j.jsb.2021.107793_b0140
  article-title: The structure, function, and mechanical properties of keratin
  publication-title: JOM
  doi: 10.1007/s11837-012-0302-8
  contributor:
    fullname: McKittrick
– volume: 23
  start-page: 801
  year: 2006
  ident: 10.1016/j.jsb.2021.107793_b0015
  article-title: Distribution and characterization of keratins in the epidermis of the tuatara (Sphenodon punctatus)
  publication-title: Zool. Sci.
  doi: 10.2108/zsj.23.801
  contributor:
    fullname: Alibardi
– ident: 10.1016/j.jsb.2021.107793_b0130
  doi: 10.1126/science.aan6398
– volume: 314B
  start-page: 11
  year: 2010
  ident: 10.1016/j.jsb.2021.107793_b0045
  article-title: Forty keratin-associated beta-proteins (β-proteins) form the hard layers of scales, claws, adhesive pads in the green anole lizard
  publication-title: Anolis carolinensis. J. Exp. Zool
  doi: 10.1002/jez.b.21306
  contributor:
    fullname: Dalla Valle
– volume: 137
  start-page: 128
  issue: 1-2
  year: 2002
  ident: 10.1016/j.jsb.2021.107793_b0185
  article-title: Sequence comparisons of intermediate filament chains: evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1
  publication-title: J. Struct. Biol.
  doi: 10.1006/jsbi.2002.4438
  contributor:
    fullname: Smith
– volume: 212
  year: 2020
  ident: 10.1016/j.jsb.2021.107793_b0145
  article-title: Structure and topology of the linkers in the conserved lepidosaur β-keratin chain with four 34-residue repeats support an interfilament role for the central linker
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2020.107599
  contributor:
    fullname: Parry
– volume: 110
  start-page: 1199
  year: 1990
  ident: 10.1016/j.jsb.2021.107793_b0110
  article-title: The coiled-coil of in vitro assembled keratin filaments is a heterodimer of Type I and II keratin: use of site-specific mutagenesis and recombinant protein expression
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.110.4.1199
  contributor:
    fullname: Hatzfeld
– volume: 15
  start-page: 82
  year: 2015
  ident: 10.1016/j.jsb.2021.107793_b0215
  article-title: Convergent evolution of cysteine-rich proteins in feathers and hair
  publication-title: BMC Evol. Biol.
  doi: 10.1186/s12862-015-0360-y
  contributor:
    fullname: Strasser
– volume: 122
  start-page: E6770
  year: 2015
  ident: 10.1016/j.jsb.2021.107793_b0245
  article-title: Topographical mapping of α- and β-keratins on developing chicken skin integument: functional interaction and evolutionary perspectives
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Wu
– volume: 10
  start-page: 148
  issue: 1
  year: 2010
  ident: 10.1016/j.jsb.2021.107793_b0095
  article-title: Genomic organization and molecular phylogenies of the beta (β) keratin multigene family in the chicken (Gallus gallus) and zebra finch (Taeniopygia guttata): implications for feather evolution
  publication-title: BMC Evol. Biol.
  doi: 10.1186/1471-2148-10-148
  contributor:
    fullname: Greenwold
– ident: 10.1016/j.jsb.2021.107793_b0070
  doi: 10.1007/978-3-319-49674-0_8
– volume: 12
  start-page: 771
  year: 2013
  ident: 10.1016/j.jsb.2021.107793_b0180
  article-title: Chicken corneocyte cross-linked proteome
  publication-title: J. Proteome Res.
  doi: 10.1021/pr301036k
  contributor:
    fullname: Rice
– volume: 32
  start-page: 1792
  issue: 5
  year: 2004
  ident: 10.1016/j.jsb.2021.107793_b0055
  article-title: MUSCLE: multiple sequence alignment with high accuracy and high throughput
  publication-title: Nucl. Acids Res.
  doi: 10.1093/nar/gkh340
  contributor:
    fullname: Edgar
– volume: 215
  start-page: 161
  year: 1990
  ident: 10.1016/j.jsb.2021.107793_b0025
  article-title: High-resolution spot-scan electron microscopy of microcrystals of an α-helical coiled-coil protein
  publication-title: J. Mol. Biol.
  doi: 10.1016/S0022-2836(05)80101-9
  contributor:
    fullname: Bullough
– volume: 32
  start-page: 99
  year: 1999
  ident: 10.1016/j.jsb.2021.107793_b0160
  article-title: Intermediate Filaments: Molecular Architecture, Assembly, Dynamics and Polymorphism
  publication-title: Q. Rev. Biophys.
  doi: 10.1017/S0033583500003516
  contributor:
    fullname: Parry
– volume: 124
  start-page: 4221
  year: 2011
  ident: 10.1016/j.jsb.2021.107793_b0220
  article-title: Unique amino acid signatures that are evolutionarily conserved distinguish simple-type, epidermal and hair keratins
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.089516
  contributor:
    fullname: Strnad
– ident: 10.1016/j.jsb.2021.107793_b0080
  doi: 10.1007/978-981-10-8195-8_6
– volume: 83
  start-page: 19
  year: 2004
  ident: 10.1016/j.jsb.2021.107793_b0120
  article-title: Comprehensive analysis of keratin gene clusters in humans and rodents
  publication-title: Eur. J. Cell Biol.
  doi: 10.1078/0171-9335-00354
  contributor:
    fullname: Hesse
– volume: 25
  start-page: 1189
  year: 2009
  ident: 10.1016/j.jsb.2021.107793_b0240
  article-title: Jalview version 2 - a multiple sequence alignment editor and analysis workbench
  publication-title: Bioinformatics.
  doi: 10.1093/bioinformatics/btp033
  contributor:
    fullname: Waterhouse
– volume: 477
  start-page: 587
  year: 2011
  ident: 10.1016/j.jsb.2021.107793_b0005
  article-title: The genome of the green anole lizard and a comparative analysis with birds and mammals
  publication-title: Nature
  doi: 10.1038/nature10390
  contributor:
    fullname: Alföldi
– volume: 29
  start-page: 995
  year: 2012
  ident: 10.1016/j.jsb.2021.107793_b0225
  article-title: Radiation and functional diversification of alpha keratins during early vertebrate evolution
  publication-title: Mol. Biol. Evol.
  doi: 10.1093/molbev/msr269
  contributor:
    fullname: Vandebergh
– volume: 105
  start-page: 18419
  year: 2008
  ident: 10.1016/j.jsb.2021.107793_b0050
  article-title: Identification of reptilian genes encoding hair keratin-like proteins suggests a new scenario for the evolutionary origin of hair
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0805154105
  contributor:
    fullname: Eckhart
– volume: 200
  start-page: 45
  year: 2017
  ident: 10.1016/j.jsb.2021.107793_b0075
  article-title: Intermediate filament structure in fully differentiated (oxidised) trichocyte keratin
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2017.09.003
  contributor:
    fullname: Fraser
– volume: 127
  start-page: 1012
  year: 1985
  ident: 10.1016/j.jsb.2021.107793_b0175
  article-title: The coiled-coil molecules of intermediate filaments consist of two parallel chains in exact axial register
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/S0006-291X(85)80045-0
  contributor:
    fullname: Parry
– volume: 274
  start-page: 9881
  issue: 14
  year: 1999
  ident: 10.1016/j.jsb.2021.107793_b0210
  article-title: A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a type VI intermediate filament protein: limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV α-internexin
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.274.14.9881
  contributor:
    fullname: Steinert
– volume: 5
  start-page: 267
  year: 1983
  ident: 10.1016/j.jsb.2021.107793_b0035
  article-title: Structure of intermediate filaments
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/0141-8130(83)90040-5
  contributor:
    fullname: Crewther
– volume: 330
  start-page: 438
  year: 2018
  ident: 10.1016/j.jsb.2021.107793_b0125
  article-title: Review: Evolution and diversification of corneous beta-proteins, the characteristic epidermal proteins of reptiles and birds
  publication-title: J. Exp. Zool. (Mol. Dev. Evol.)
  doi: 10.1002/jez.b.22840
  contributor:
    fullname: Holthaus
– volume: 37
  start-page: 982
  year: 2020
  ident: 10.1016/j.jsb.2021.107793_b0060
  article-title: Convergent evolution of cysteine-rich keratins in hard skin appendages of terrestrial vertebrates
  publication-title: Mol. Biol. Evol.
  doi: 10.1093/molbev/msz279
  contributor:
    fullname: Ehrlich
– ident: 10.1016/j.jsb.2021.107793_b0135
  doi: 10.1016/S0065-3233(06)73001-7
– volume: 327
  start-page: 263
  year: 2016
  ident: 10.1016/j.jsb.2021.107793_b0010
  article-title: The process of cornification evolved from the initial keratinization in the epidermis and epidermal derivatives of vertebrates: a new synthesis and the case of sauropsids
  publication-title: Int. Rev. Cell Mol. Biol.
  doi: 10.1016/bs.ircmb.2016.06.005
  contributor:
    fullname: Alibardi
– volume: 584
  start-page: 403
  year: 2020
  ident: 10.1016/j.jsb.2021.107793_b0090
  article-title: The tuatara genome reveals ancient features of amniote evolution
  publication-title: Nature
  doi: 10.1038/s41586-020-2561-9
  contributor:
    fullname: Gemmell
– volume: 32
  start-page: 10046
  issue: 38
  year: 1993
  ident: 10.1016/j.jsb.2021.107793_b0205
  article-title: Conservation of the structure of keratin intermediate filaments: molecular mechanism by which different keratin molecules integrate into pre-existing keratin intermediate filaments during differentiation
  publication-title: Biochem.
  doi: 10.1021/bi00089a021
  contributor:
    fullname: Steinert
– volume: 12
  start-page: 591
  year: 2021
  ident: 10.1016/j.jsb.2021.107793_b0150
  article-title: Structures of the β-keratin filaments and keratin intermediate filaments in the epidermal appendages of birds and reptiles (sauropsids)
  publication-title: Genes.
  doi: 10.3390/genes12040591
  contributor:
    fullname: Parry
– volume: 192
  start-page: 528
  year: 2015
  ident: 10.1016/j.jsb.2021.107793_b0065
  article-title: The molecular structure of the silk fibers from Hymenoptera aculeata (bees, wasps, ants)
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2015.10.017
  contributor:
    fullname: Fraser
– volume: 76
  start-page: 229
  year: 2016
  ident: 10.1016/j.jsb.2021.107793_b0230
  article-title: Keratin: structure, mechanical properties, occurrence in biological organisms and efforts in bioinspiration
  publication-title: Progr. Mater. Sci.
  doi: 10.1016/j.pmatsci.2015.06.001
  contributor:
    fullname: Wang
– volume: 151
  start-page: 1459
  year: 2000
  ident: 10.1016/j.jsb.2021.107793_b0235
  article-title: In vitro assembly and structure of trichocyte keratin intermediate filaments: a novel role for stabilization by disulfide bonding
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.151.7.1459
  contributor:
    fullname: Wang
– volume: 320B
  start-page: 393
  year: 2013
  ident: 10.1016/j.jsb.2021.107793_b0100
  article-title: Molecular evolution and expression of archosaurian β-keratins and the origin of feather β-keratins
  publication-title: J. Exp. Zool. Mol. Dev. Evol.
  doi: 10.1002/jez.b.22514
  contributor:
    fullname: Greenwold
– start-page: 1
  year: 1995
  ident: 10.1016/j.jsb.2021.107793_b0155
  contributor:
    fullname: Parry
– ident: 10.1016/j.jsb.2021.107793_b0165
  doi: 10.1016/j.jsb.2021.107706
– ident: 10.1016/j.jsb.2021.107793_b0020
  doi: 10.1073/pnas.1820320116
– volume: 14
  start-page: 249
  year: 2014
  ident: 10.1016/j.jsb.2021.107793_b0105
  article-title: Dynamic evolution of the alpha (α) and beta (β) keratins has accompanied integument diversification and the adaption of birds into novel lifestyles
  publication-title: BMC Evol. Biol.
  doi: 10.1186/s12862-014-0249-1
  contributor:
    fullname: Greenwold
– year: 1972
  ident: 10.1016/j.jsb.2021.107793_b0085
  contributor:
    fullname: Fraser
– volume: 84
  start-page: 623
  year: 2005
  ident: 10.1016/j.jsb.2021.107793_b0255
  article-title: Terrestrial vertebrates have two keratin gene clusters: striking differences in teleost fish
  publication-title: Eur. J. Cell Biol.
  doi: 10.1016/j.ejcb.2005.01.007
  contributor:
    fullname: Zimek
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Snippet •Sequences of 28 Type I and II KIF chains in common wall lizard.•Type I and II genes lie in clusters on chromosomes 13 and 2 respectively.•Heads and tails of...
On the basis of sequence homology with mammalian α-keratins, and on the criteria that the coiled-coil segments and central linker in the rod domain of these...
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StartPage 107793
SubjectTerms Amino Acid Sequence
Animals
Cysteine - chemistry
Cysteine - genetics
Cysteine - metabolism
Cytoskeleton - metabolism
Epidermal appendages
Epidermis - metabolism
Epithelium - metabolism
Filament crosslinker
Glycine - chemistry
Glycine - genetics
Glycine - metabolism
Intermediate Filaments - chemistry
Intermediate Filaments - genetics
Intermediate Filaments - metabolism
Keratin intermediate filament chains
Keratins - chemistry
Keratins - genetics
Keratins - metabolism
Lizard keratin
Lizards - classification
Lizards - genetics
Lizards - metabolism
Multigene Family - genetics
Proline - chemistry
Proline - genetics
Proline - metabolism
Sequence Homology, Amino Acid
Sequence repeats
Species Specificity
Title Keratin intermediate filament chains in the European common wall lizard (Podarcis muralis) and a potential keratin filament crosslinker
URI https://dx.doi.org/10.1016/j.jsb.2021.107793
https://www.ncbi.nlm.nih.gov/pubmed/34481988
https://search.proquest.com/docview/2569614303
Volume 213
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