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...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2023-03-01
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| Series: | FEBS Open Bio |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/2211-5463.13560 |
| _version_ | 1811158673949458432 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-04-10T05:28:08Z |
| format | Article |
| id | doaj.art-88bd6d7f694942fd983f90b3246b7dab |
| institution | Directory Open Access Journal |
| issn | 2211-5463 |
| language | English |
| last_indexed | 2024-04-10T05:28:08Z |
| publishDate | 2023-03-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj.art-88bd6d7f694942fd983f90b3246b7dab2023-03-07T09:42:22ZengWileyFEBS Open Bio2211-54632023-03-0113350051010.1002/2211-5463.13560Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp.Trang Hoang0ChanSu Jeong1Sei‐Heon Jang2ChangWoo Lee3Department of Biomedical Science and Center for Bio‐Nanomaterials Daegu University Gyeongsan South KoreaDepartment of Biomedical Science and Center for Bio‐Nanomaterials Daegu University Gyeongsan South KoreaDepartment of Biomedical Science and Center for Bio‐Nanomaterials Daegu University Gyeongsan South KoreaDepartment of Biomedical Science and Center for Bio‐Nanomaterials Daegu University Gyeongsan South KoreaGlutaredoxins (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.https://doi.org/10.1002/2211-5463.13560aromatic amino acidscis‐proline loopcold adaptationglutaredoxinhydrogen bond networkthioredoxin‐fold |
| spellingShingle | 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. FEBS Open Bio aromatic amino acids cis‐proline loop cold adaptation glutaredoxin hydrogen bond network thioredoxin‐fold |
| 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_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_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_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 |
| topic | aromatic amino acids cis‐proline loop cold adaptation glutaredoxin hydrogen bond network thioredoxin‐fold |
| url | https://doi.org/10.1002/2211-5463.13560 |
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