Histidine Patch Thioredoxins
A cluster of surface amino acid residues on Escherichia coli thioredoxin were systematically mutated in order to provide the molecule with an ability to chelate metal ions. The combined effect of two histidine mutants, E30H and Q62H, gave thioredoxin the capacity to bind to nickel ions immobilized o...
Saved in:
| Published in | The Journal of biological chemistry Vol. 271; no. 9; pp. 5059 - 5065 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
American Society for Biochemistry and Molecular Biology
01.03.1996
|
| Online Access | Get full text |
Cover
Loading…
| Abstract | A cluster of surface amino acid residues on Escherichia coli thioredoxin were systematically mutated in order to provide the molecule with an ability to chelate metal ions. The combined
effect of two histidine mutants, E30H and Q62H, gave thioredoxin the capacity to bind to nickel ions immobilized on iminodiacetic
acid- and nitrilotriacetic acid-Sepharose resins. Even though these two histidines were more than 30 residues apart in thioredoxin's
primary sequence, they were found to satisfy the geometric constraints for metal ion coordination as a result of the thioredoxin
tertiary fold. A third histidine mutation, S1H, provided additional metal ion chelation affinity, but the native histidine
at position 6 of thioredoxin was found not to participate in binding. All of the histidine mutants exhibited decreased thermal
stability as compared with wild-type thioredoxin; however, the introduction of an additional mutation, D26A, increased their
melting temperatures beyond that of wild-type thioredoxin. The metal chelating abilities of these histidine mutants of thioredoxin
were successfully utilized for convenient purifications of human interleukin-8 and â11 expressed in E. coli as soluble thioredoxin fusion proteins. |
|---|---|
| AbstractList | A cluster of surface amino acid residues on Escherichia coli thioredoxin were systematically mutated in order to provide the molecule with an ability to chelate metal ions. The combined
effect of two histidine mutants, E30H and Q62H, gave thioredoxin the capacity to bind to nickel ions immobilized on iminodiacetic
acid- and nitrilotriacetic acid-Sepharose resins. Even though these two histidines were more than 30 residues apart in thioredoxin's
primary sequence, they were found to satisfy the geometric constraints for metal ion coordination as a result of the thioredoxin
tertiary fold. A third histidine mutation, S1H, provided additional metal ion chelation affinity, but the native histidine
at position 6 of thioredoxin was found not to participate in binding. All of the histidine mutants exhibited decreased thermal
stability as compared with wild-type thioredoxin; however, the introduction of an additional mutation, D26A, increased their
melting temperatures beyond that of wild-type thioredoxin. The metal chelating abilities of these histidine mutants of thioredoxin
were successfully utilized for convenient purifications of human interleukin-8 and â11 expressed in E. coli as soluble thioredoxin fusion proteins. |
| Author | Nicholas W. Warne Maximillian T. Follettie Kathleen L. Grant John M. McCoy Zhijian Lu Elizabeth A. DiBlasio-Smith Mark J. Williamson Edward R. LaVallie Lisa A. Collins-Racie |
| Author_xml | – sequence: 1 givenname: Zhijian surname: Lu fullname: Lu, Zhijian – sequence: 2 givenname: Elizabeth A. surname: DiBlasio-Smith fullname: DiBlasio-Smith, Elizabeth A. – sequence: 3 givenname: Kathleen L. surname: Grant fullname: Grant, Kathleen L. – sequence: 4 givenname: Nicholas W. surname: Warne fullname: Warne, Nicholas W. – sequence: 5 givenname: Edward R. surname: LaVallie fullname: LaVallie, Edward R. – sequence: 6 givenname: Lisa A. surname: Collins-Racie fullname: Collins-Racie, Lisa A. – sequence: 7 givenname: Maximillian T. surname: Follettie fullname: Follettie, Maximillian T. – sequence: 8 givenname: Mark J. surname: Williamson fullname: Williamson, Mark J. – sequence: 9 givenname: John M. surname: McCoy fullname: McCoy, John M. |
| BookMark | eNpNj01LAzEYhINU6rZ69eSheN-YNx-b5CjFWqGghwrewubLTbG7khTUf--WenAuc5kZ5pmhST_0AaFrIBiI5Hc76zCVgDUWROgzVAFRrGYC3iaoIoRCralQF2hWyo6M4hqmaKoakFKxCt2sUzkkn_qweGkPrltsuzTk4Ifv1JdLdB7bjxKu_nyOXlcP2-W63jw_Pi3vN7UDAbq2QlKuGhY8B8cC9baJTja6Ua0CHYFEyoGyyNrAnbdej--YI15xpa3TlM0RPu26PJSSQzSfOe3b_GOAmCOlGSnNSGm0OVKOhdtToUvv3VfKwdg0uC7s_4d-AQwXT10 |
| CitedBy_id | crossref_primary_10_1016_j_bpc_2024_107271 crossref_primary_10_1093_protein_14_5_367 crossref_primary_10_1039_C4MT00222A crossref_primary_10_1016_j_pep_2005_01_013 crossref_primary_10_1002_pro_4150 crossref_primary_10_1016_j_cca_2015_07_008 crossref_primary_10_1042_BA20020043 crossref_primary_10_1002_0471140864_ps0607s10 crossref_primary_10_1016_S0021_9673_00_00886_4 crossref_primary_10_1016_j_mser_2008_04_004 crossref_primary_10_1242_dev_126_7_1467 crossref_primary_10_1016_j_jmb_2007_09_074 crossref_primary_10_1016_S1570_0232_01_00637_7 crossref_primary_10_1016_S0168_583X_03_00988_1 crossref_primary_10_1016_j_pep_2013_11_007 crossref_primary_10_1074_jbc_M005642200 crossref_primary_10_1111_j_1399_3011_1998_tb00624_x crossref_primary_10_1016_S0141_0229_00_00215_5 crossref_primary_10_7717_peerj_2714 crossref_primary_10_1006_exer_1997_0418 crossref_primary_10_1016_S0969_2126_02_00752_9 crossref_primary_10_1038_nature02158 crossref_primary_10_1016_j_pep_2005_08_017 crossref_primary_10_1016_S1389_0344_02_00050_3 crossref_primary_10_1110_ps_8_8_1668 crossref_primary_10_1007_s10969_005_9003_7 crossref_primary_10_1006_prep_1997_0767 crossref_primary_10_1016_j_reactfunctpolym_2009_07_001 crossref_primary_10_1016_S0167_4838_99_00235_6 crossref_primary_10_1006_prep_2001_1465 crossref_primary_10_1006_exer_2001_1031 crossref_primary_10_1016_S0303_7207_98_00097_5 crossref_primary_10_1002_jmr_555 crossref_primary_10_1016_S0969_2126_00_00193_3 crossref_primary_10_1002_ceat_200500144 crossref_primary_10_1074_jbc_272_44_27529 crossref_primary_10_1093_nar_26_6_1414 crossref_primary_10_1016_j_pep_2005_08_009 crossref_primary_10_1101_pdb_top102129 crossref_primary_10_1074_jbc_M505736200 crossref_primary_10_1128_JVI_73_6_4582_4589_1999 crossref_primary_10_1016_j_procbio_2014_12_001 |
| Cites_doi | 10.1021/bi00080a026 10.1016/S0021-9258(19)49464-7 10.1016/0958-1669(95)80083-2 10.1016/0378-1119(88)90005-4 10.1111/j.1749-6632.1995.tb32323.x 10.1021/ja00995a002 10.1016/S0021-9673(00)93969-4 10.1021/bi00028a001 10.1038/258598a0 10.1093/protein/6.1.109 10.1038/309810a0 10.1021/bi00469a016 10.1016/0022-2836(90)90313-B 10.1016/0003-2697(87)90587-2 10.1021/bi00005a036 10.1016/0378-1119(88)90004-2 10.1016/1046-5928(92)90001-D 10.1093/protein/7.9.1115 10.1107/S0021889891004399 10.1038/nbt1088-1204 10.1128/jb.176.2.359-367.1994 10.1093/intimm/5.2.233 10.1021/bi00244a032 |
| ContentType | Journal Article |
| DBID | AAYXX CITATION |
| DOI | 10.1074/jbc.271.9.5059 |
| DatabaseName | CrossRef |
| DatabaseTitle | CrossRef |
| DatabaseTitleList | |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Anatomy & Physiology Chemistry |
| EISSN | 1083-351X |
| EndPage | 5065 |
| ExternalDocumentID | 10_1074_jbc_271_9_5059 271_9_5059 |
| GroupedDBID | - 02 08R 186 2WC 3O- 53G 55 5BI 5GY 5RE 5VS 85S AARDX AAWZA ABFLS ABOCM ABPPZ ABPTK ABUFD ABZEH ACDCL ACNCT ADACO ADBBV ADBIT ADCOW AEILP AENEX AFFNX AFMIJ AIZTS ALMA_UNASSIGNED_HOLDINGS C1A CJ0 CS3 DIK DL DU5 DZ E3Z EBS EJD ET F20 F5P FA8 FH7 FRP GJ GX1 H13 HH5 IH2 J5H KM KQ8 L7B LI MVM MYA N9A NHB O0- OHM OHT OK1 P-O P0W P2P R.V RHF RHI RNS RPM SJN TBC TN5 UHB UPT UQL VH1 VQA WH7 WOQ X X7M XFK XHC XJT Y6R YZZ ZA5 ZGI ZY4 --- -DZ -ET -~X .55 .GJ 0R~ 0SF 18M 29J 34G 39C 4.4 41~ 6TJ 79B AAEDW AAFWJ AALRI AAXUO AAYJJ AAYOK AAYXX ABDNZ ABFSI ABRJW ABTAH ACGFO ACSFO ACYGS ADIYS ADNWM ADVLN AEXQZ AFOSN AFPKN AI. AITUG AKRWK AMRAJ AOIJS BAWUL BTFSW CITATION E.L FDB GROUPED_DOAJ HYE QZG ROL TR2 UKR W8F WHG XSW YQT YSK YWH YYP ZE2 ~02 ~KM |
| ID | FETCH-LOGICAL-c1519-b5724863ed41c3e2db6fc76968a819f10f24123f3ae4cdbd93513c0d8489bc923 |
| ISSN | 0021-9258 |
| IngestDate | Fri Aug 23 02:59:48 EDT 2024 Tue Jan 05 14:53:59 EST 2021 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 9 |
| Language | English |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c1519-b5724863ed41c3e2db6fc76968a819f10f24123f3ae4cdbd93513c0d8489bc923 |
| OpenAccessLink | http://www.jbc.org/article/S0021925818825509/pdf |
| PMID | 8617783 |
| PageCount | 7 |
| ParticipantIDs | crossref_primary_10_1074_jbc_271_9_5059 highwire_biochem_271_9_5059 |
| ProviderPackageCode | RHF RHI |
| PublicationCentury | 1900 |
| PublicationDate | 19960301 1996-03-00 |
| PublicationDateYYYYMMDD | 1996-03-01 |
| PublicationDate_xml | – month: 03 year: 1996 text: 19960301 day: 01 |
| PublicationDecade | 1990 |
| PublicationTitle | The Journal of biological chemistry |
| PublicationYear | 1996 |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher_xml | – name: American Society for Biochemistry and Molecular Biology |
| References | Smith (10.1074/jbc.271.9.5059_bib1) 1988; 67 Schmidt (10.1074/jbc.271.9.5059_bib9) 1993; 6 Dyson (10.1074/jbc.271.9.5059_bib25) 1990; 29 Chaga (10.1074/jbc.271.9.5059_bib24) 1994; 7 Williams (10.1074/jbc.271.9.5059_bib22) 1995; 34 Porath (10.1074/jbc.271.9.5059_bib12) 1992; 3 Brandts (10.1074/jbc.271.9.5059_bib19) 1967; 89 Wilson (10.1074/jbc.271.9.5059_bib27) 1995; 34 Czupryn (10.1074/jbc.271.9.5059_bib23) 1995; 762 Glusker (10.1074/jbc.271.9.5059_bib26) 1991; 42 Ladbury (10.1074/jbc.271.9.5059_bib20) 1993; 32 Hopp (10.1074/jbc.271.9.5059_bib8) 1988; 6 LaVallie (10.1074/jbc.271.9.5059_bib6) 1993; 268 Hochuli (10.1074/jbc.271.9.5059_bib10) 1988; 6 Langsetmo (10.1074/jbc.271.9.5059_bib21) 1991; 30 Collins-Racie (10.1074/jbc.271.9.5059_bib5) 1995; 13 Porath (10.1074/jbc.271.9.5059_bib11) 1975; 258 Katti (10.1074/jbc.271.9.5059_bib17) 1990; 257 Schagger (10.1074/jbc.271.9.5059_bib16) 1987; 166 Hochuli (10.1074/jbc.271.9.5059_bib18) 1987; 411 LaVallie (10.1074/jbc.271.9.5059_bib4) 1995; 6 Nagai (10.1074/jbc.271.9.5059_bib7) 1984; 309 Peitsch (10.1074/jbc.271.9.5059_bib14) 1993; 5 LaVallie (10.1074/jbc.271.9.5059_bib3) 1993; 11 Kaufmann (10.1074/jbc.271.9.5059_bib13) 1994; 176 di Guan (10.1074/jbc.271.9.5059_bib2) 1988; 67 Kraulis (10.1074/jbc.271.9.5059_bib15) 1991; 24 |
| References_xml | – volume: 32 start-page: 7526 year: 1993 ident: 10.1074/jbc.271.9.5059_bib20 publication-title: Biochemistry doi: 10.1021/bi00080a026 contributor: fullname: Ladbury – volume: 268 start-page: 23311 year: 1993 ident: 10.1074/jbc.271.9.5059_bib6 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)49464-7 contributor: fullname: LaVallie – volume: 6 start-page: 501 year: 1995 ident: 10.1074/jbc.271.9.5059_bib4 publication-title: Curr. Opin. Biotechnol. doi: 10.1016/0958-1669(95)80083-2 contributor: fullname: LaVallie – volume: 67 start-page: 31 year: 1988 ident: 10.1074/jbc.271.9.5059_bib1 publication-title: Gene (Amst.) doi: 10.1016/0378-1119(88)90005-4 contributor: fullname: Smith – volume: 762 start-page: 152 year: 1995 ident: 10.1074/jbc.271.9.5059_bib23 publication-title: Ann. N. Y. Acad. Sci. doi: 10.1111/j.1749-6632.1995.tb32323.x contributor: fullname: Czupryn – volume: 89 start-page: 4826 year: 1967 ident: 10.1074/jbc.271.9.5059_bib19 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00995a002 contributor: fullname: Brandts – volume: 42 start-page: 1 year: 1991 ident: 10.1074/jbc.271.9.5059_bib26 publication-title: Adv. Prot. Chem. contributor: fullname: Glusker – volume: 411 start-page: 177 year: 1987 ident: 10.1074/jbc.271.9.5059_bib18 publication-title: J. Chromatogr. doi: 10.1016/S0021-9673(00)93969-4 contributor: fullname: Hochuli – volume: 34 start-page: 8931 year: 1995 ident: 10.1074/jbc.271.9.5059_bib27 publication-title: Biochemistry doi: 10.1021/bi00028a001 contributor: fullname: Wilson – volume: 258 start-page: 598 year: 1975 ident: 10.1074/jbc.271.9.5059_bib11 publication-title: Nature doi: 10.1038/258598a0 contributor: fullname: Porath – volume: 6 start-page: 109 year: 1993 ident: 10.1074/jbc.271.9.5059_bib9 publication-title: Protein Eng. doi: 10.1093/protein/6.1.109 contributor: fullname: Schmidt – volume: 309 start-page: 810 year: 1984 ident: 10.1074/jbc.271.9.5059_bib7 publication-title: Nature doi: 10.1038/309810a0 contributor: fullname: Nagai – volume: 29 start-page: 4129 year: 1990 ident: 10.1074/jbc.271.9.5059_bib25 publication-title: Biochemistry doi: 10.1021/bi00469a016 contributor: fullname: Dyson – volume: 257 start-page: 167 year: 1990 ident: 10.1074/jbc.271.9.5059_bib17 publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(90)90313-B contributor: fullname: Katti – volume: 166 start-page: 368 year: 1987 ident: 10.1074/jbc.271.9.5059_bib16 publication-title: Anal. Biochem. doi: 10.1016/0003-2697(87)90587-2 contributor: fullname: Schagger – volume: 6 start-page: 1321 year: 1988 ident: 10.1074/jbc.271.9.5059_bib10 publication-title: Bio/Technology contributor: fullname: Hochuli – volume: 11 start-page: 187 year: 1993 ident: 10.1074/jbc.271.9.5059_bib3 publication-title: Bio/Technology contributor: fullname: LaVallie – volume: 34 start-page: 1787 year: 1995 ident: 10.1074/jbc.271.9.5059_bib22 publication-title: Biochemistry doi: 10.1021/bi00005a036 contributor: fullname: Williams – volume: 13 start-page: 982 year: 1995 ident: 10.1074/jbc.271.9.5059_bib5 publication-title: Bio/Technology contributor: fullname: Collins-Racie – volume: 67 start-page: 21 year: 1988 ident: 10.1074/jbc.271.9.5059_bib2 publication-title: Gene (Amst.) doi: 10.1016/0378-1119(88)90004-2 contributor: fullname: di Guan – volume: 3 start-page: 263 year: 1992 ident: 10.1074/jbc.271.9.5059_bib12 publication-title: Protein Expression Purif. doi: 10.1016/1046-5928(92)90001-D contributor: fullname: Porath – volume: 7 start-page: 1115 year: 1994 ident: 10.1074/jbc.271.9.5059_bib24 publication-title: Protein Eng. doi: 10.1093/protein/7.9.1115 contributor: fullname: Chaga – volume: 24 start-page: 946 year: 1991 ident: 10.1074/jbc.271.9.5059_bib15 publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889891004399 contributor: fullname: Kraulis – volume: 6 start-page: 1205 year: 1988 ident: 10.1074/jbc.271.9.5059_bib8 publication-title: Bio/Technology doi: 10.1038/nbt1088-1204 contributor: fullname: Hopp – volume: 176 start-page: 359 year: 1994 ident: 10.1074/jbc.271.9.5059_bib13 publication-title: J. Bacteriol. doi: 10.1128/jb.176.2.359-367.1994 contributor: fullname: Kaufmann – volume: 5 start-page: 233 year: 1993 ident: 10.1074/jbc.271.9.5059_bib14 publication-title: Int. Immunol. doi: 10.1093/intimm/5.2.233 contributor: fullname: Peitsch – volume: 30 start-page: 7603 year: 1991 ident: 10.1074/jbc.271.9.5059_bib21 publication-title: Biochemistry doi: 10.1021/bi00244a032 contributor: fullname: Langsetmo |
| SSID | ssj0000491 |
| Score | 1.5299859 |
| Snippet | A cluster of surface amino acid residues on Escherichia coli thioredoxin were systematically mutated in order to provide the molecule with an ability to... |
| SourceID | crossref highwire |
| SourceType | Aggregation Database Publisher |
| StartPage | 5059 |
| Title | Histidine Patch Thioredoxins |
| URI | http://www.jbc.org/content/271/9/5059.abstract |
| Volume | 271 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3PS8MwFA46D3oRdYpzU3oQPYzW_kjX5jinMvyFgmO7lTRN2QZuohuof70vTdNmuoN6KaUhKe37ePmSvPc9hI5Dn6c-E0HtNmUm5g43aSslJk9pECc-j8PsxPTuvtXt4euBP9AyrkV2ySy22OfSvJL_WBWegV1FluwfLFsMCg_gHuwLV7AwXH9lY6HxMUoET3wAjzoURTinQgD0fZTvwY1LLGjMUwovSWkQVe-tCMyZZ8cVw9FYw83F6FxkW07NYh-miAZrtq0yhIdKEQMVodG8Ldr6NN86BeSJ1fRbs2-VGw4yRllFXBUJAI5JXKm4rpyoGzgaWojmEoFiEW169W1ZG-KH6wYuI1x3zCwYyyJW2U_XyP42dxURhdlZeoAj6B9B_4hEov8qWnMD4otF-c1jqSIPqyJZSTH_ECXmGeCzxfcvkhUlIK0RkKcttJnbz2hLGGyjFT7ZQdX2hM6mzx_GiZHF8maHJDtovaPsWkWNAiVGhhJDR8ku6l1dPnW6Zl4Tw2TAzYgZ-4GLw5bHE-wwj7tJlqwlFI4ocLvUsVOgZK6XepRjlsQJ8XzHY3YS4pDEDNj8HqpMphO-jwzMhUMPmR3wFIuVKwsp0HvH5S6lLZvV0Kn6-OhFSp9Ey39zDdXVv4kAwgK6WuvBr8epo40ScA1Umb3O-SFwvll8lBnwCw6GU3I |
| link.rule.ids | 315,786,790,27957,27958 |
| linkProvider | Colorado Alliance of Research Libraries |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Histidine+Patch+Thioredoxins&rft.jtitle=The+Journal+of+biological+chemistry&rft.au=Lu%2C+Zhijian&rft.au=DiBlasio-Smith%2C+Elizabeth+A.&rft.au=Grant%2C+Kathleen+L.&rft.au=Warne%2C+Nicholas+W.&rft.date=1996-03-01&rft.issn=0021-9258&rft.volume=271&rft.issue=9&rft.spage=5059&rft.epage=5065&rft_id=info:doi/10.1074%2Fjbc.271.9.5059&rft.externalDBID=n%2Fa&rft.externalDocID=10_1074_jbc_271_9_5059 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0021-9258&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0021-9258&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0021-9258&client=summon |