Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp.
Glutaredoxins (Grxs) are small proteins that share a well‐conserved thioredoxin (Trx)‐fold and participate in many biological processes. This study examined the cold adaptation mechanism of a Fe‐S cluster binding class II Grx4 (SpGrx4) from the psychrophilic Arctic bacterium Sphingomonas sp. PAMC 26...
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Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9989929/ http://www.ncbi.nlm.nih.gov/pubmed/36680400 https://doi.org/10.1002/2211-5463.13560 |
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ftpubmed:oai:pubmedcentral.nih.gov:9989929 2023-05-15T14:58:48+02:00 Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp. Hoang, Trang Jeong, ChanSu Jang, Sei‐Heon Lee, ChangWoo 2023-01-29 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9989929/ http://www.ncbi.nlm.nih.gov/pubmed/36680400 https://doi.org/10.1002/2211-5463.13560 en eng John Wiley and Sons Inc. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9989929/ http://www.ncbi.nlm.nih.gov/pubmed/36680400 http://dx.doi.org/10.1002/2211-5463.13560 © 2023 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. FEBS Open Bio Research Articles Text 2023 ftpubmed https://doi.org/10.1002/2211-5463.13560 2023-03-12T02:08:09Z Glutaredoxins (Grxs) are small proteins that share a well‐conserved thioredoxin (Trx)‐fold and participate in many biological processes. This study examined the cold adaptation mechanism of a Fe‐S cluster binding class II Grx4 (SpGrx4) from the psychrophilic Arctic bacterium Sphingomonas sp. PAMC 26621. Three polar residues close to the cis‐proline residue (P73) of SpGrx4 form a hydrogen bond network (Q74–S67–Y76) with the cis‐proline loop main chain. The hydroxyl group of S67 or Y76 or both is replaced in similar Grxs depending on the temperature of the habitat. Mutants with reduced hydrogen bonds (S67A, Q74A, Y76F, and S67A/Y76W) were more susceptible to urea‐induced unfolding and more flexible than the wild‐type (WT). By contrast, Y76W, with a bulky indole group, was the most stable. These mutants showed higher melting temperatures than WT as a consequence of increased hydrophobic interactions. These results suggest that the tyrosine residue, Y76, is preferred for the cold adaptation of SpGrx4 with a heat‐labile structure despite the rigid cis‐proline loop, due to hydrogen bond formation. An aromatic residue on β3 (cis‐proline plus3) modulates the stability‐flexibility of the cis‐proline loop for temperature adaptation of prokaryotic class II Grx4 members via hydrogen bonds and hydrophobic interactions. Text Arctic PubMed Central (PMC) Arctic FEBS Open Bio 13 3 500 510 |
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Research Articles Hoang, Trang Jeong, ChanSu Jang, Sei‐Heon Lee, ChangWoo Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp. |
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Research Articles |
description |
Glutaredoxins (Grxs) are small proteins that share a well‐conserved thioredoxin (Trx)‐fold and participate in many biological processes. This study examined the cold adaptation mechanism of a Fe‐S cluster binding class II Grx4 (SpGrx4) from the psychrophilic Arctic bacterium Sphingomonas sp. PAMC 26621. Three polar residues close to the cis‐proline residue (P73) of SpGrx4 form a hydrogen bond network (Q74–S67–Y76) with the cis‐proline loop main chain. The hydroxyl group of S67 or Y76 or both is replaced in similar Grxs depending on the temperature of the habitat. Mutants with reduced hydrogen bonds (S67A, Q74A, Y76F, and S67A/Y76W) were more susceptible to urea‐induced unfolding and more flexible than the wild‐type (WT). By contrast, Y76W, with a bulky indole group, was the most stable. These mutants showed higher melting temperatures than WT as a consequence of increased hydrophobic interactions. These results suggest that the tyrosine residue, Y76, is preferred for the cold adaptation of SpGrx4 with a heat‐labile structure despite the rigid cis‐proline loop, due to hydrogen bond formation. An aromatic residue on β3 (cis‐proline plus3) modulates the stability‐flexibility of the cis‐proline loop for temperature adaptation of prokaryotic class II Grx4 members via hydrogen bonds and hydrophobic interactions. |
format |
Text |
author |
Hoang, Trang Jeong, ChanSu Jang, Sei‐Heon Lee, ChangWoo |
author_facet |
Hoang, Trang Jeong, ChanSu Jang, Sei‐Heon Lee, ChangWoo |
author_sort |
Hoang, Trang |
title |
Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp. |
title_short |
Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp. |
title_full |
Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp. |
title_fullStr |
Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp. |
title_full_unstemmed |
Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp. |
title_sort |
tyr76 is essential for the cold adaptation of a class ii glutaredoxin 4 with a heat‐labile structure from the arctic bacterium sphingomonas sp. |
publisher |
John Wiley and Sons Inc. |
publishDate |
2023 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9989929/ http://www.ncbi.nlm.nih.gov/pubmed/36680400 https://doi.org/10.1002/2211-5463.13560 |
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Arctic |
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Arctic |
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Arctic |
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Arctic |
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FEBS Open Bio |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9989929/ http://www.ncbi.nlm.nih.gov/pubmed/36680400 http://dx.doi.org/10.1002/2211-5463.13560 |
op_rights |
© 2023 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
op_doi |
https://doi.org/10.1002/2211-5463.13560 |
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500 |
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510 |
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