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A non-canonical multisubunit RNA polymerase encoded by a giant bacteriophage

The infection of Pseudomonas aeruginosa by the giant bacteriophage phiKZ is resistant to host RNA polymerase (RNAP) inhibitor rifampicin. phiKZ encodes two sets of polypeptides that are distantly related to fragments of the two largest subunits of cellular multisubunit RNAPs. Polypeptides of one set...

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Autores principales: Yakunina, Maria, Artamonova, Tatyana, Borukhov, Sergei, Makarova, Kira S., Severinov, Konstantin, Minakhin, Leonid
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4666361/
https://www.ncbi.nlm.nih.gov/pubmed/26490960
http://dx.doi.org/10.1093/nar/gkv1095
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author Yakunina, Maria
Artamonova, Tatyana
Borukhov, Sergei
Makarova, Kira S.
Severinov, Konstantin
Minakhin, Leonid
author_facet Yakunina, Maria
Artamonova, Tatyana
Borukhov, Sergei
Makarova, Kira S.
Severinov, Konstantin
Minakhin, Leonid
author_sort Yakunina, Maria
collection PubMed
description The infection of Pseudomonas aeruginosa by the giant bacteriophage phiKZ is resistant to host RNA polymerase (RNAP) inhibitor rifampicin. phiKZ encodes two sets of polypeptides that are distantly related to fragments of the two largest subunits of cellular multisubunit RNAPs. Polypeptides of one set are encoded by middle phage genes and are found in the phiKZ virions. Polypeptides of the second set are encoded by early phage genes and are absent from virions. Here, we report isolation of a five-subunit RNAP from phiKZ-infected cells. Four subunits of this enzyme are cellular RNAP subunits homologs of the non-virion set; the fifth subunit is a protein of unknown function. In vitro, this complex initiates transcription from late phiKZ promoters in rifampicin-resistant manner. Thus, this enzyme is a non-virion phiKZ RNAP responsible for transcription of late phage genes. The phiKZ RNAP lacks identifiable assembly and promoter specificity subunits/factors characteristic for eukaryal, archaeal and bacterial RNAPs and thus provides a unique model for comparative analysis of the mechanism, regulation and evolution of this important class of enzymes.
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spelling pubmed-46663612015-12-02 A non-canonical multisubunit RNA polymerase encoded by a giant bacteriophage Yakunina, Maria Artamonova, Tatyana Borukhov, Sergei Makarova, Kira S. Severinov, Konstantin Minakhin, Leonid Nucleic Acids Res Nucleic Acid Enzymes The infection of Pseudomonas aeruginosa by the giant bacteriophage phiKZ is resistant to host RNA polymerase (RNAP) inhibitor rifampicin. phiKZ encodes two sets of polypeptides that are distantly related to fragments of the two largest subunits of cellular multisubunit RNAPs. Polypeptides of one set are encoded by middle phage genes and are found in the phiKZ virions. Polypeptides of the second set are encoded by early phage genes and are absent from virions. Here, we report isolation of a five-subunit RNAP from phiKZ-infected cells. Four subunits of this enzyme are cellular RNAP subunits homologs of the non-virion set; the fifth subunit is a protein of unknown function. In vitro, this complex initiates transcription from late phiKZ promoters in rifampicin-resistant manner. Thus, this enzyme is a non-virion phiKZ RNAP responsible for transcription of late phage genes. The phiKZ RNAP lacks identifiable assembly and promoter specificity subunits/factors characteristic for eukaryal, archaeal and bacterial RNAPs and thus provides a unique model for comparative analysis of the mechanism, regulation and evolution of this important class of enzymes. Oxford University Press 2015-12-02 2015-10-20 /pmc/articles/PMC4666361/ /pubmed/26490960 http://dx.doi.org/10.1093/nar/gkv1095 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Nucleic Acid Enzymes
Yakunina, Maria
Artamonova, Tatyana
Borukhov, Sergei
Makarova, Kira S.
Severinov, Konstantin
Minakhin, Leonid
A non-canonical multisubunit RNA polymerase encoded by a giant bacteriophage
title A non-canonical multisubunit RNA polymerase encoded by a giant bacteriophage
title_full A non-canonical multisubunit RNA polymerase encoded by a giant bacteriophage
title_fullStr A non-canonical multisubunit RNA polymerase encoded by a giant bacteriophage
title_full_unstemmed A non-canonical multisubunit RNA polymerase encoded by a giant bacteriophage
title_short A non-canonical multisubunit RNA polymerase encoded by a giant bacteriophage
title_sort non-canonical multisubunit rna polymerase encoded by a giant bacteriophage
topic Nucleic Acid Enzymes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4666361/
https://www.ncbi.nlm.nih.gov/pubmed/26490960
http://dx.doi.org/10.1093/nar/gkv1095
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