Analysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2).
In this work we report a detailed analysis of the topology and phylogenetics of family 2 glycoside hydrolases (GH2). We distinguish five topologies or domain architectures based on the presence and distribution of protein domains defined in Pfam and Interpro databases. All of them share a central TI...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2016-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC5145203?pdf=render |
| _version_ | 1828785567782928384 |
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| author | David Talens-Perales Anna Górska Daniel H Huson Julio Polaina Julia Marín-Navarro |
| author_facet | David Talens-Perales Anna Górska Daniel H Huson Julio Polaina Julia Marín-Navarro |
| author_sort | David Talens-Perales |
| collection | DOAJ |
| description | In this work we report a detailed analysis of the topology and phylogenetics of family 2 glycoside hydrolases (GH2). We distinguish five topologies or domain architectures based on the presence and distribution of protein domains defined in Pfam and Interpro databases. All of them share a central TIM barrel (catalytic module) with two β-sandwich domains (non-catalytic) at the N-terminal end, but differ in the occurrence and nature of additional non-catalytic modules at the C-terminal region. Phylogenetic analysis was based on the sequence of the Pfam Glyco_hydro_2_C catalytic module present in most GH2 proteins. Our results led us to propose a model in which evolutionary diversity of GH2 enzymes is driven by the addition of different non-catalytic domains at the C-terminal region. This model accounts for the divergence of β-galactosidases from β-glucuronidases, the diversification of β-galactosidases with different transglycosylation specificities, and the emergence of bicistronic β-galactosidases. This study also allows the identification of groups of functionally uncharacterized protein sequences with potential biotechnological interest. |
| first_indexed | 2024-12-11T23:54:45Z |
| format | Article |
| id | doaj.art-77c0f9dbd32643b390dc9869d09fa40e |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T23:54:45Z |
| publishDate | 2016-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-77c0f9dbd32643b390dc9869d09fa40e2022-12-22T00:45:23ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-011112e016803510.1371/journal.pone.0168035Analysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2).David Talens-PeralesAnna GórskaDaniel H HusonJulio PolainaJulia Marín-NavarroIn this work we report a detailed analysis of the topology and phylogenetics of family 2 glycoside hydrolases (GH2). We distinguish five topologies or domain architectures based on the presence and distribution of protein domains defined in Pfam and Interpro databases. All of them share a central TIM barrel (catalytic module) with two β-sandwich domains (non-catalytic) at the N-terminal end, but differ in the occurrence and nature of additional non-catalytic modules at the C-terminal region. Phylogenetic analysis was based on the sequence of the Pfam Glyco_hydro_2_C catalytic module present in most GH2 proteins. Our results led us to propose a model in which evolutionary diversity of GH2 enzymes is driven by the addition of different non-catalytic domains at the C-terminal region. This model accounts for the divergence of β-galactosidases from β-glucuronidases, the diversification of β-galactosidases with different transglycosylation specificities, and the emergence of bicistronic β-galactosidases. This study also allows the identification of groups of functionally uncharacterized protein sequences with potential biotechnological interest.http://europepmc.org/articles/PMC5145203?pdf=render |
| spellingShingle | David Talens-Perales Anna Górska Daniel H Huson Julio Polaina Julia Marín-Navarro Analysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2). PLoS ONE |
| title | Analysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2). |
| title_full | Analysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2). |
| title_fullStr | Analysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2). |
| title_full_unstemmed | Analysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2). |
| title_short | Analysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2). |
| title_sort | analysis of domain architecture and phylogenetics of family 2 glycoside hydrolases gh2 |
| url | http://europepmc.org/articles/PMC5145203?pdf=render |
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