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: | https://doi.org/10.1002/2211-5463.13560 https://doaj.org/article/88bd6d7f694942fd983f90b3246b7dab |
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ftdoajarticles:oai:doaj.org/article:88bd6d7f694942fd983f90b3246b7dab 2023-05-15T14:59:22+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. Trang Hoang ChanSu Jeong Sei‐Heon Jang ChangWoo Lee 2023-03-01T00:00:00Z https://doi.org/10.1002/2211-5463.13560 https://doaj.org/article/88bd6d7f694942fd983f90b3246b7dab EN eng Wiley https://doi.org/10.1002/2211-5463.13560 https://doaj.org/toc/2211-5463 2211-5463 doi:10.1002/2211-5463.13560 https://doaj.org/article/88bd6d7f694942fd983f90b3246b7dab FEBS Open Bio, Vol 13, Iss 3, Pp 500-510 (2023) aromatic amino acids cis‐proline loop cold adaptation glutaredoxin hydrogen bond network thioredoxin‐fold Biology (General) QH301-705.5 article 2023 ftdoajarticles https://doi.org/10.1002/2211-5463.13560 2023-03-12T01:33:34Z 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. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic FEBS Open Bio 13 3 500 510 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
aromatic amino acids cis‐proline loop cold adaptation glutaredoxin hydrogen bond network thioredoxin‐fold Biology (General) QH301-705.5 |
spellingShingle |
aromatic amino acids cis‐proline loop cold adaptation glutaredoxin hydrogen bond network thioredoxin‐fold Biology (General) QH301-705.5 Trang Hoang ChanSu Jeong Sei‐Heon Jang ChangWoo Lee Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp. |
topic_facet |
aromatic amino acids cis‐proline loop cold adaptation glutaredoxin hydrogen bond network thioredoxin‐fold Biology (General) QH301-705.5 |
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 |
Article in Journal/Newspaper |
author |
Trang Hoang ChanSu Jeong Sei‐Heon Jang ChangWoo Lee |
author_facet |
Trang Hoang ChanSu Jeong Sei‐Heon Jang ChangWoo Lee |
author_sort |
Trang Hoang |
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 |
Wiley |
publishDate |
2023 |
url |
https://doi.org/10.1002/2211-5463.13560 https://doaj.org/article/88bd6d7f694942fd983f90b3246b7dab |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
FEBS Open Bio, Vol 13, Iss 3, Pp 500-510 (2023) |
op_relation |
https://doi.org/10.1002/2211-5463.13560 https://doaj.org/toc/2211-5463 2211-5463 doi:10.1002/2211-5463.13560 https://doaj.org/article/88bd6d7f694942fd983f90b3246b7dab |
op_doi |
https://doi.org/10.1002/2211-5463.13560 |
container_title |
FEBS Open Bio |
container_volume |
13 |
container_issue |
3 |
container_start_page |
500 |
op_container_end_page |
510 |
_version_ |
1766331472896065536 |