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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2015
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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. |
format | Online Article Text |
id | pubmed-4666361 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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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