Implications of divergence of methionine adenosyltransferase in archaea
Methionine adenosyltransferase (MAT) catalyzes the biosynthesis of S‐adenosyl methionine from l‐methionine and ATP. MAT enzymes are ancient, believed to share a common ancestor, and are highly conserved in all three domains of life. However, the sequences of archaeal MATs show considerable divergenc...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2022-01-01
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| Series: | FEBS Open Bio |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/2211-5463.13312 |
| _version_ | 1818974234576158720 |
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| author | Bhanu Pratap Singh Chouhan Madhuri Gade Desirae Martinez Saacnicteh Toledo‐Patino Paola Laurino |
| author_facet | Bhanu Pratap Singh Chouhan Madhuri Gade Desirae Martinez Saacnicteh Toledo‐Patino Paola Laurino |
| author_sort | Bhanu Pratap Singh Chouhan |
| collection | DOAJ |
| description | Methionine adenosyltransferase (MAT) catalyzes the biosynthesis of S‐adenosyl methionine from l‐methionine and ATP. MAT enzymes are ancient, believed to share a common ancestor, and are highly conserved in all three domains of life. However, the sequences of archaeal MATs show considerable divergence compared with their bacterial and eukaryotic counterparts. Furthermore, the structural significance and functional significance of this sequence divergence are not well understood. In the present study, we employed structural analysis and ancestral sequence reconstruction to investigate archaeal MAT divergence. We observed that the dimer interface containing the active site (which is usually well conserved) diverged considerably between the bacterial/eukaryotic MATs and archaeal MAT. A detailed investigation of the available structures supports the sequence analysis outcome: The protein domains and subdomains of bacterial and eukaryotic MAT are more similar than those of archaea. Finally, we resurrected archaeal MAT ancestors. Interestingly, archaeal MAT ancestors show substrate specificity, which is lost during evolution. This observation supports the hypothesis of a common MAT ancestor for the three domains of life. In conclusion, we have demonstrated that archaeal MAT is an ideal system for studying an enzyme family that evolved differently in one domain compared with others while maintaining the same catalytic activity. |
| first_indexed | 2024-12-20T15:36:49Z |
| format | Article |
| id | doaj.art-0442df84847c4cd681036442ebe4ccb9 |
| institution | Directory Open Access Journal |
| issn | 2211-5463 |
| language | English |
| last_indexed | 2024-12-20T15:36:49Z |
| publishDate | 2022-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj.art-0442df84847c4cd681036442ebe4ccb92022-12-21T19:35:23ZengWileyFEBS Open Bio2211-54632022-01-0112113014510.1002/2211-5463.13312Implications of divergence of methionine adenosyltransferase in archaeaBhanu Pratap Singh Chouhan0Madhuri Gade1Desirae Martinez2Saacnicteh Toledo‐Patino3Paola Laurino4Protein Engineering and Evolution Unit Okinawa Institute of Science and Technology Graduate University Onna JapanProtein Engineering and Evolution Unit Okinawa Institute of Science and Technology Graduate University Onna JapanProtein Engineering and Evolution Unit Okinawa Institute of Science and Technology Graduate University Onna JapanProtein Engineering and Evolution Unit Okinawa Institute of Science and Technology Graduate University Onna JapanProtein Engineering and Evolution Unit Okinawa Institute of Science and Technology Graduate University Onna JapanMethionine adenosyltransferase (MAT) catalyzes the biosynthesis of S‐adenosyl methionine from l‐methionine and ATP. MAT enzymes are ancient, believed to share a common ancestor, and are highly conserved in all three domains of life. However, the sequences of archaeal MATs show considerable divergence compared with their bacterial and eukaryotic counterparts. Furthermore, the structural significance and functional significance of this sequence divergence are not well understood. In the present study, we employed structural analysis and ancestral sequence reconstruction to investigate archaeal MAT divergence. We observed that the dimer interface containing the active site (which is usually well conserved) diverged considerably between the bacterial/eukaryotic MATs and archaeal MAT. A detailed investigation of the available structures supports the sequence analysis outcome: The protein domains and subdomains of bacterial and eukaryotic MAT are more similar than those of archaea. Finally, we resurrected archaeal MAT ancestors. Interestingly, archaeal MAT ancestors show substrate specificity, which is lost during evolution. This observation supports the hypothesis of a common MAT ancestor for the three domains of life. In conclusion, we have demonstrated that archaeal MAT is an ideal system for studying an enzyme family that evolved differently in one domain compared with others while maintaining the same catalytic activity.https://doi.org/10.1002/2211-5463.13312ancestral sequence reconstructioncatalytic interfacedivergenceenzyme evolutionmethionine adenosyltransferase |
| spellingShingle | Bhanu Pratap Singh Chouhan Madhuri Gade Desirae Martinez Saacnicteh Toledo‐Patino Paola Laurino Implications of divergence of methionine adenosyltransferase in archaea FEBS Open Bio ancestral sequence reconstruction catalytic interface divergence enzyme evolution methionine adenosyltransferase |
| title | Implications of divergence of methionine adenosyltransferase in archaea |
| title_full | Implications of divergence of methionine adenosyltransferase in archaea |
| title_fullStr | Implications of divergence of methionine adenosyltransferase in archaea |
| title_full_unstemmed | Implications of divergence of methionine adenosyltransferase in archaea |
| title_short | Implications of divergence of methionine adenosyltransferase in archaea |
| title_sort | implications of divergence of methionine adenosyltransferase in archaea |
| topic | ancestral sequence reconstruction catalytic interface divergence enzyme evolution methionine adenosyltransferase |
| url | https://doi.org/10.1002/2211-5463.13312 |
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