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Co-evolution of RNA polymerase with RbpA in the phylum Actinobacteria

The role of RbpA in the backdrop of M. smegmatis showed that it rescues mycobacterial RNA polymerase from rifampicin-mediated inhibition (Dey et al., 2010; Dey et al., 2011). Paget and co-workers (Paget et al., 2001; Newell et al., 2006) have revealed that RbpA homologs occur exclusively in actinoba...

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Detalles Bibliográficos
Autores principales: Dey, Abhinav, Adithi, V.R., Chatterji, Dipankar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5121209/
https://www.ncbi.nlm.nih.gov/pubmed/27896048
http://dx.doi.org/10.1016/j.atg.2012.03.001
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author Dey, Abhinav
Adithi, V.R.
Chatterji, Dipankar
author_facet Dey, Abhinav
Adithi, V.R.
Chatterji, Dipankar
author_sort Dey, Abhinav
collection PubMed
description The role of RbpA in the backdrop of M. smegmatis showed that it rescues mycobacterial RNA polymerase from rifampicin-mediated inhibition (Dey et al., 2010; Dey et al., 2011). Paget and co-workers (Paget et al., 2001; Newell et al., 2006) have revealed that RbpA homologs occur exclusively in actinobacteria. Newell et al. (2006) showed that MtbRbpA, when complemented in a ∆rbpA mutant of S. coelicolor, showed a low recovery of MIC (from 0.75 to 2 μg/ml) as compared to complementation by native RbpA of S. coelicolor (MIC increases from 0.75 to 11 μg/ml). Our studies on MsRbpA show that it is a differential marker for M. smegmatis RNA polymerase as compared to E. coli RNA polymerase at IC(50) levels of rifampicin. A recent sequence-based analysis by Lane and Darst (2010) has shown that RNA polymerases from Proteobacteria and Actinobacteria have had a divergent evolution. E. coli is a representative of Proteobacteria and M. smegmatis is an Actinobacterium. RbpA has an exclusive occurrence in Actinobacteria. Since protein–protein interactions might not be conserved across different species, therefore, the probable reason for the indifference of MsRbpA toward E. coli RNA polymerase could be the lineage-specific differences between actinobacterial and proteobacterial RNA polymerases. These observations led us to ask the question as to whether the evolution of RbpA in Actinobacteria followed the same route as that of RNA polymerase subunits from actinobacterial species. We show that the exclusivity of RbpA in Actinobacteria and the unique evolution of RNA polymerase in this phylum share a co-evolutionary link. We have addressed this issue by a blending of experimental and bioinformatics based approaches. They comprise of induction of bacterial cultures coupled to rifampicin-tolerance, transcription assays and statistical comparison of phylogenetic trees for different pairs of proteins in actinobacteria.
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spelling pubmed-51212092016-11-28 Co-evolution of RNA polymerase with RbpA in the phylum Actinobacteria Dey, Abhinav Adithi, V.R. Chatterji, Dipankar Appl Transl Genom Article The role of RbpA in the backdrop of M. smegmatis showed that it rescues mycobacterial RNA polymerase from rifampicin-mediated inhibition (Dey et al., 2010; Dey et al., 2011). Paget and co-workers (Paget et al., 2001; Newell et al., 2006) have revealed that RbpA homologs occur exclusively in actinobacteria. Newell et al. (2006) showed that MtbRbpA, when complemented in a ∆rbpA mutant of S. coelicolor, showed a low recovery of MIC (from 0.75 to 2 μg/ml) as compared to complementation by native RbpA of S. coelicolor (MIC increases from 0.75 to 11 μg/ml). Our studies on MsRbpA show that it is a differential marker for M. smegmatis RNA polymerase as compared to E. coli RNA polymerase at IC(50) levels of rifampicin. A recent sequence-based analysis by Lane and Darst (2010) has shown that RNA polymerases from Proteobacteria and Actinobacteria have had a divergent evolution. E. coli is a representative of Proteobacteria and M. smegmatis is an Actinobacterium. RbpA has an exclusive occurrence in Actinobacteria. Since protein–protein interactions might not be conserved across different species, therefore, the probable reason for the indifference of MsRbpA toward E. coli RNA polymerase could be the lineage-specific differences between actinobacterial and proteobacterial RNA polymerases. These observations led us to ask the question as to whether the evolution of RbpA in Actinobacteria followed the same route as that of RNA polymerase subunits from actinobacterial species. We show that the exclusivity of RbpA in Actinobacteria and the unique evolution of RNA polymerase in this phylum share a co-evolutionary link. We have addressed this issue by a blending of experimental and bioinformatics based approaches. They comprise of induction of bacterial cultures coupled to rifampicin-tolerance, transcription assays and statistical comparison of phylogenetic trees for different pairs of proteins in actinobacteria. Elsevier 2012-05-26 /pmc/articles/PMC5121209/ /pubmed/27896048 http://dx.doi.org/10.1016/j.atg.2012.03.001 Text en © 2012 Elsevier B.V. http://creativecommons.org/licenses/by-nc-nd/3.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).
spellingShingle Article
Dey, Abhinav
Adithi, V.R.
Chatterji, Dipankar
Co-evolution of RNA polymerase with RbpA in the phylum Actinobacteria
title Co-evolution of RNA polymerase with RbpA in the phylum Actinobacteria
title_full Co-evolution of RNA polymerase with RbpA in the phylum Actinobacteria
title_fullStr Co-evolution of RNA polymerase with RbpA in the phylum Actinobacteria
title_full_unstemmed Co-evolution of RNA polymerase with RbpA in the phylum Actinobacteria
title_short Co-evolution of RNA polymerase with RbpA in the phylum Actinobacteria
title_sort co-evolution of rna polymerase with rbpa in the phylum actinobacteria
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5121209/
https://www.ncbi.nlm.nih.gov/pubmed/27896048
http://dx.doi.org/10.1016/j.atg.2012.03.001
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