Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif
Small heat shock proteins (sHSPs) play a central role in protein homeostasis under conditions of stress by binding partly unfolded, aggregate‐prone proteins and keeping them soluble. Like many sHSPs, the widely expressed human sHSP, αB‐crystallin (‘αB’), forms large polydisperse multimeric assemblie...
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| Published in | The EMBO journal Vol. 31; no. 24; pp. 4587 - 4594 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
12.12.2012
Nature Publishing Group UK Nature Publishing Group |
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| Online Access | Get full text |
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| Abstract | Small heat shock proteins (sHSPs) play a central role in protein homeostasis under conditions of stress by binding partly unfolded, aggregate‐prone proteins and keeping them soluble. Like many sHSPs, the widely expressed human sHSP, αB‐crystallin (‘αB’), forms large polydisperse multimeric assemblies. Molecular interactions involved in both sHSP function and oligomer formation remain to be delineated. A growing database of structural information reveals that a central conserved α‐crystallin domain (ACD) forms dimeric building blocks, while flanking N‐ and C‐termini direct the formation of larger sHSP oligomers. The most commonly observed inter‐subunit interaction involves a highly conserved C‐terminal ‘IxI/V’ motif and a groove in the ACD that is also implicated in client binding. To investigate the inherent properties of this interaction, peptides mimicking the IxI/V motif of αB and other human sHSPs were tested for binding to dimeric αB‐ACD. IxI‐mimicking peptides bind the isolated ACD at 22°C in a manner similar to interactions observed in the oligomer at low temperature, confirming these interactions are likely to exist in functional αB oligomers.
Cytoprotective small heat‐shock proteins display an intrinsic affinity for their C‐termini in solution, providing candidate binding sites for both sHSP function and oligomerization. |
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| AbstractList | Small heat shock proteins (sHSPs) play a central role in protein homeostasis under conditions of stress by binding partly unfolded, aggregate-prone proteins and keeping them soluble. Like many sHSPs, the widely expressed human sHSP, αB-crystallin ('αB'), forms large polydisperse multimeric assemblies. Molecular interactions involved in both sHSP function and oligomer formation remain to be delineated. A growing database of structural information reveals that a central conserved α-crystallin domain (ACD) forms dimeric building blocks, while flanking N- and C-termini direct the formation of larger sHSP oligomers. The most commonly observed inter-subunit interaction involves a highly conserved C-terminal 'IxI/V' motif and a groove in the ACD that is also implicated in client binding. To investigate the inherent properties of this interaction, peptides mimicking the IxI/V motif of αB and other human sHSPs were tested for binding to dimeric αB-ACD. IxI-mimicking peptides bind the isolated ACD at 22°C in a manner similar to interactions observed in the oligomer at low temperature, confirming these interactions are likely to exist in functional αB oligomers.Small heat shock proteins (sHSPs) play a central role in protein homeostasis under conditions of stress by binding partly unfolded, aggregate-prone proteins and keeping them soluble. Like many sHSPs, the widely expressed human sHSP, αB-crystallin ('αB'), forms large polydisperse multimeric assemblies. Molecular interactions involved in both sHSP function and oligomer formation remain to be delineated. A growing database of structural information reveals that a central conserved α-crystallin domain (ACD) forms dimeric building blocks, while flanking N- and C-termini direct the formation of larger sHSP oligomers. The most commonly observed inter-subunit interaction involves a highly conserved C-terminal 'IxI/V' motif and a groove in the ACD that is also implicated in client binding. To investigate the inherent properties of this interaction, peptides mimicking the IxI/V motif of αB and other human sHSPs were tested for binding to dimeric αB-ACD. IxI-mimicking peptides bind the isolated ACD at 22°C in a manner similar to interactions observed in the oligomer at low temperature, confirming these interactions are likely to exist in functional αB oligomers. Small heat shock proteins (sHSPs) play a central role in protein homeostasis under conditions of stress by binding partly unfolded, aggregate-prone proteins and keeping them soluble. Like many sHSPs, the widely expressed human sHSP, αB-crystallin (‘αB'), forms large polydisperse multimeric assemblies. Molecular interactions involved in both sHSP function and oligomer formation remain to be delineated. A growing database of structural information reveals that a central conserved α-crystallin domain (ACD) forms dimeric building blocks, while flanking N- and C-termini direct the formation of larger sHSP oligomers. The most commonly observed inter-subunit interaction involves a highly conserved C-terminal ‘IxI/V' motif and a groove in the ACD that is also implicated in client binding. To investigate the inherent properties of this interaction, peptides mimicking the IxI/V motif of αB and other human sHSPs were tested for binding to dimeric αB-ACD. IxI-mimicking peptides bind the isolated ACD at 22°C in a manner similar to interactions observed in the oligomer at low temperature, confirming these interactions are likely to exist in functional αB oligomers. Cytoprotective small heat-shock proteins display an intrinsic affinity for their C-termini in solution, providing candidate binding sites for both sHSP function and oligomerization. Small heat shock proteins (sHSPs) play a central role in protein homeostasis under conditions of stress by binding partly unfolded, aggregate-prone proteins and keeping them soluble. Like many sHSPs, the widely expressed human sHSP, αB-crystallin ('αB'), forms large polydisperse multimeric assemblies. Molecular interactions involved in both sHSP function and oligomer formation remain to be delineated. A growing database of structural information reveals that a central conserved α-crystallin domain (ACD) forms dimeric building blocks, while flanking N- and C-termini direct the formation of larger sHSP oligomers. The most commonly observed inter-subunit interaction involves a highly conserved C-terminal 'IxI/V' motif and a groove in the ACD that is also implicated in client binding. To investigate the inherent properties of this interaction, peptides mimicking the IxI/V motif of αB and other human sHSPs were tested for binding to dimeric αB-ACD. IxI-mimicking peptides bind the isolated ACD at 22°C in a manner similar to interactions observed in the oligomer at low temperature, confirming these interactions are likely to exist in functional αB oligomers. |
| Author | Jehle, Stefan Klevit, Rachel Delbecq, Scott P |
| Author_xml | – sequence: 1 givenname: Scott P surname: Delbecq fullname: Delbecq, Scott P organization: Department of Biochemistry, University of Washington, WA, Seattle, USA – sequence: 2 givenname: Stefan surname: Jehle fullname: Jehle, Stefan organization: Department of Biochemistry, University of Washington, WA, Seattle, USA – sequence: 3 givenname: Rachel surname: Klevit fullname: Klevit, Rachel email: klevit@uw.edu organization: Department of Biochemistry, University of Washington, WA, Seattle, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23188086$$D View this record in MEDLINE/PubMed |
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Nat Strucl Mol Biol 17: 1037-1042 Johnson BA, Blevins RA (1994) NMR View: A computer program for the visualization and analysis of NMR data. J Biomol NMR 4: 603-614 Brady JP, Garland DL, Green DE, Tamm ER, Giblin FJ, Wawrousek EF (2001) AlphaB-crystallin in lens development and muscle integrity: a gene knockout approach. Invest Ophthalmol Vis Sci 42: 2924-2934 Bukau B, Weissman J, Horwich A (2006) Molecular chaperones and protein quality control. Cell 125: 443-451 Kim KK, Kim R, Kim SH (1998) Crystal structure of a small heat-shock protein. Nature 394: 595-599 Studer S, Obrist M, Lentze N, Narberhaus F (2002) A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins. Eur J Biochem 269: 3578-3586 Bagnéris C, Bateman OA, Naylor CE, Cronin N, Boelens WC, Keep NH, Slingsby C (2009) Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. J Mol Biol 392: 1242-1252 Braun N, Zacharias M, Peschek J, Kastenmüller A, Zou J, Hanzlik M, Haslbeck M, Rappsilber J, Buchner J, Weinkauf S (2011) Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach. Proc Natl Acad Sci USA 108: 20491-20496 Vicart P, Caron A, Guicheney P, Li Z, Prévost MC, Faure A, Chateau D, Chapon F, Tomé F, Dupret JM, Paulin D, Fardeau M (1998) A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet 20: 92-95 Aquilina JA, Benesch JL, Bateman OA, Slingsby C, Robinson CV (2003) Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin. Proc Natl Acad Sci USA 19: 10611-10616 Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipeL a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293 Treweek TM, Rekas A, Walker MJ, Carver JA (2010) A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin. Exp Eye Res 91: 691-699 Baldwin AJ, Hilton GR, Lioe H, Bagneris C, Benesch JLP, Kay LE (2011) Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus. J Mol Biol 413: 310-320 Langanowsky A, Benesch J, Landau M, Ding L, Sawaya M, Cascio D, Huang Q, Robinson C, Horwitz J, Eisenberg D (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci 19: 1031-1043 Moyano JV, Evans JR, Chen F, Lu M, Werner ME, Yehiely F, Diaz LK, Turbin D, Karaca G, Wiley E, Nielsen TO, Perou CM, Cryns VL (2006) AlphaB-crystallin is a novel oncoprotein that predicts poor clinical outcome in breast cancer. J Clin Invest 116: 261-270 Liu Y, Zhang X, Luo L, Wu M, Zeng R, Cheng G, Hu B, Liu B, Liang JJ, Shang F (2006) A novel αB-crystallin mutation associated with autosomal dominant congenital lamellar cataract. Invest Ophthalmol Vis Sci 47: 1069-1075 Taylor RP, Benjamin IKJ (2005) Small heat shock proteins: a new classification scheme in mammals. J Mol Cell Cardiol 38: 433-444 Bukach OV, Glukhova AE, Seit-Nebi AS, Gusev NB (2009) Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20). Biochim Biophys Acta 1794: 486-495 Stamler R, Kappe G, Boelens W, Slingsby C (2005) Wrapping the α-Crystallin Domain Fold in a Chaperone Assembly. J Mol Biol 353: 68-79 Takeda K, Hayashi T, Abe T, Hirano Y, Hanazono Y, Yohda M, Miki K (2011) Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0. J Struct Biol 174: 92-99 Selcen D, Engel AG (2003) Myofibrillar myopathy caused by novel dominant negative α B-crystallin mutations. Ann Neurol 54: 804-810 Hayes VH, Devlin G, Quinlan RA (2008) Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells. J Biol Chem 283: 10500-10512 Ray PS, Martin JL, Swanson EA, Otani H, Dillmann WH, Das DK (2001) Transgene overexpression of alphaB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion. FASEB J 15: 393-402 Vargas-Roig LM, Gago FE, Tello O, Aznar JC, Ciocca DR (1998) Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy. Int J Cancer 79: 468-475 Benesch, Aquilina, Baldwin, Rekas, Stengel, Lindner, Basha, Devlin, Horwitz, Vierling, Carver, Robinson (CR6) 2010; 17 Bukau, Weissman, Horwich (CR10) 2006; 125 Goldstein, Muffat, Cherny, Moir, Ericsson, Huang, Mavros, Coccia, Faget, Fitch, Masters, Tanzi, Chylack, Bush (CR15) 2003; 361 Rajasekaran, Connell, Christians, Yan, Taylor, Orosz, Zhang, Stevenson, Peshock, Leopold, Barry, Loscalzo, Odelberg, Benjamin (CR32) 2007; 130 Langanowsky, Benesch, Landau, Ding, Sawaya, Cascio, Huang, Robinson, Horwitz, Eisenberg (CR27) 2010; 19 Hilario, Javier, Martin, Bertolini, Fan (CR18) 2011; 408 Sugiyama, Suzuki, Kishikawa, Akutsu, Hirose, Waye, Tsui, Yoshida, Ohno (CR37) 2000; 275 Sun, Liang (CR38) 1998; 273 Brady, Garland, Green, Tamm, Giblin, Wawrousek (CR7) 2001; 42 Jehle, van Rossum, Stout, Noguchi, Falber, Rehbein, Oschkinat, Klevit, Rajagopal (CR21) 2009; 385 Bagnéris, Bateman, Naylor, Cronin, Boelens, Keep, Slingsby (CR2) 2009; 392 Kim, Kim, Kim (CR26) 1998; 394 Treweek, Rekas, Walker, Carver (CR40) 2010; 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6 Liu, Zhang, Luo, Wu, Zeng, Cheng, Hu, Liu, Liang, Shang (CR28) 2006; 47 Pasta, Raman, Ramakrishna, Rao (CR30) 2004; 10 Haslbeck, Franzmann, Weinfurtner, Buchner (CR16) 2005; 12 Johnson, Blevins (CR23) 1994; 4 van Montfort, Basha, Friedrich, Slingsby, Vierling (CR41) 2001; 8 Zantema, Verlaan‐De Vries, Maasdam, Bol, van der Eb (CR44) 1992; 267 Moyano, Evans, Chen, Lu, Werner, Yehiely, Diaz, Turbin, Karaca, Wiley, Nielsen, Perou, Cryns (CR29) 2006; 116 Vicart, Caron, Guicheney, Li, Prévost, Faure, Chateau, Chapon, Tomé, Dupret, Paulin, Fardeau (CR43) 1998; 20 Kato, Goto, Inaguma, Hasegawa, Morishita, Asano (CR24) 1994; 269 Horwitz (CR19) 1992; 89 Engelsman, Boros, Dankers, Kamps, Vree Egberts, Böde, Lane, Aquilina, Benesch, Robinson, de Jong, Boelens (CR13) 2009; 393 Selcen, Engel (CR34) 2003; 54 Baranova, Weeks, Beelen, Bukach, Gusev, Strelkov (CR5) 2011; 411 Baldwin, Lioe, Hilton, Baker, Rubinstein, Kay, Benesch (CR4) 2011; 19 Baldwin, Hilton, Lioe, Bagneris, Benesch, Kay (CR3) 2011; 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| SubjectTerms | alpha-Crystallin B Chain - isolation & purification alpha-Crystallin B Chain - metabolism alpha-crystallin domain Amino Acid Motifs - genetics Amino Acid Motifs - physiology EMBO31 EMBO40 Heat-Shock Proteins, Small - metabolism HSPB5 Humans IxI motif Nuclear Magnetic Resonance, Biomolecular Peptides - genetics Peptides - metabolism Protein Binding Protein Multimerization - physiology Protein Structure, Tertiary Protein Subunits - metabolism small heat shock protein Temperature αB-crystallin |
| Title | Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif |
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