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A non-canonical multisubunit RNA polymerase encoded by a giant bacteriophage
Author(s) -
Maria Yakunina,
Т. О. Артамонова,
Sergei Borukhov,
Kira S. Makarova,
Konstantin Severinov,
Leonid Minakhin
Publication year - 2015
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/gkv1095
Subject(s) - biology , rna polymerase , bacteriophage , transcription (linguistics) , gene , bacterial transcription , polymerase , protein subunit , genetics , rna dependent rna polymerase , rna , promoter , dna , microbiology and biotechnology , gene expression , escherichia coli , linguistics , philosophy
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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