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The phage N4 virion RNA polymerase catalytic domain is related to single‐subunit RNA polymerases
Author(s) -
Kazmierczak K.M.,
Davydova E.K.,
Mustaev A.A.,
RothmanDenes L.B.
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdf584
Subject(s) - biology , polymerase , rna dependent rna polymerase , rna polymerase i , rna polymerase , rna , microbiology and biotechnology , rna editing , protein subunit , genetics , dna , gene
In vitro , bacteriophage N4 virion RNA polymerase (vRNAP) recognizes in vivo sites of transcription initiation on single‐stranded templates. N4 vRNAP promoters are comprised of a hairpin structure and conserved sequences. Here, we show that vRNAP consists of a single 3500 amino acid polypeptide, and we define and characterize a transcriptionally active 1106 amino acid domain (mini‐vRNAP). Biochemical and genetic characterization of this domain indicates that, despite its peculiar promoter specificity and lack of extensive sequence similarity to other DNA‐dependent RNA polymerases, mini‐vRNAP is related to the family of T7‐like RNA polymerases.

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