Evolutionary Implications and Physicochemical Analyses of Selected Proteins of Type III Polyketide Synthase Family
Type III polyketide synthases have a substantial role in the biosynthesis of various polyketides in plants and microorganisms. Comparative proteomic analysis of type III polyketide synthases showed evolutionarily and structurally related positions in a compilation of amino acid sequences from differ...
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doaj-8b57966e84cd48c4a68cbbde91b539ca2020-11-25T02:23:02ZengSAGE PublishingEvolutionary Bioinformatics1176-93432011-01-01710.4137/EBO.S6854Evolutionary Implications and Physicochemical Analyses of Selected Proteins of Type III Polyketide Synthase FamilyV. Mallika0K.C. Sivakumar1E.V. Soniya2Plant Molecular Biology, Rajiv Gandhi Centre for Biotechnology, Thycaud P O, Poojappura, Thiruvananthapuram-695 014, Kerala, India.Bioinformatics facility, Rajiv Gandhi Centre for Biotechnology, Thycaud P O, Poojappura, Thiruvananthapuram-695 014, Kerala, India.Plant Molecular Biology, Rajiv Gandhi Centre for Biotechnology, Thycaud P O, Poojappura, Thiruvananthapuram-695 014, Kerala, India.Type III polyketide synthases have a substantial role in the biosynthesis of various polyketides in plants and microorganisms. Comparative proteomic analysis of type III polyketide synthases showed evolutionarily and structurally related positions in a compilation of amino acid sequences from different families. Bacterial and fungal type III polyketide synthase proteins showed <50% similarity but in higher plants, it exhibited >80% among chalcone synthases and >70% in the case of non-chalcone synthases. In a consensus phylogenetic tree based on 1000 replicates; bacterial, fungal and plant proteins were clustered in separate groups. Proteins from bryophytes and pteridophytes grouped immediately near to the fungal cluster, demonstrated how evolutionary lineage has occurred among type III polyketide synthase proteins. Upon physicochemical analysis, it was observed that the proteins localized in the cytoplasm and were hydrophobic in nature. Molecular structural analysis revealed comparatively stable structure comprising of alpha helices and random coils as major structural components. It was found that there was a decline in the structural stability with active site mutation as prophesied by the in silico mutation studies.https://doi.org/10.4137/EBO.S6854 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
V. Mallika K.C. Sivakumar E.V. Soniya |
spellingShingle |
V. Mallika K.C. Sivakumar E.V. Soniya Evolutionary Implications and Physicochemical Analyses of Selected Proteins of Type III Polyketide Synthase Family Evolutionary Bioinformatics |
author_facet |
V. Mallika K.C. Sivakumar E.V. Soniya |
author_sort |
V. Mallika |
title |
Evolutionary Implications and Physicochemical Analyses of Selected Proteins of Type III Polyketide Synthase Family |
title_short |
Evolutionary Implications and Physicochemical Analyses of Selected Proteins of Type III Polyketide Synthase Family |
title_full |
Evolutionary Implications and Physicochemical Analyses of Selected Proteins of Type III Polyketide Synthase Family |
title_fullStr |
Evolutionary Implications and Physicochemical Analyses of Selected Proteins of Type III Polyketide Synthase Family |
title_full_unstemmed |
Evolutionary Implications and Physicochemical Analyses of Selected Proteins of Type III Polyketide Synthase Family |
title_sort |
evolutionary implications and physicochemical analyses of selected proteins of type iii polyketide synthase family |
publisher |
SAGE Publishing |
series |
Evolutionary Bioinformatics |
issn |
1176-9343 |
publishDate |
2011-01-01 |
description |
Type III polyketide synthases have a substantial role in the biosynthesis of various polyketides in plants and microorganisms. Comparative proteomic analysis of type III polyketide synthases showed evolutionarily and structurally related positions in a compilation of amino acid sequences from different families. Bacterial and fungal type III polyketide synthase proteins showed <50% similarity but in higher plants, it exhibited >80% among chalcone synthases and >70% in the case of non-chalcone synthases. In a consensus phylogenetic tree based on 1000 replicates; bacterial, fungal and plant proteins were clustered in separate groups. Proteins from bryophytes and pteridophytes grouped immediately near to the fungal cluster, demonstrated how evolutionary lineage has occurred among type III polyketide synthase proteins. Upon physicochemical analysis, it was observed that the proteins localized in the cytoplasm and were hydrophobic in nature. Molecular structural analysis revealed comparatively stable structure comprising of alpha helices and random coils as major structural components. It was found that there was a decline in the structural stability with active site mutation as prophesied by the in silico mutation studies. |
url |
https://doi.org/10.4137/EBO.S6854 |
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