The phage N4 virion RNA polymerase catalytic domain is related to single-subunit RNA polymerases.
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.
Kazmierczak
K M
KM
Department of Molecular Genetics and Cell Biology, The University of Chicago, 920 East 58th Street, IL 60637, USA.
Davydova
E K
EK
Mustaev
A A
AA
Rothman-Denes
L B
LB
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D025522:Bacteriophage N4 / Q000201:enzymology*; D001483:Base Sequence; D020134:Catalytic Domain; D003001:Cloning, Molecular; D017931:DNA Primers; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010802:Phylogeny; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014771:Virion / Q000201:enzymology*
D017931:DNA Primers; D011994:Recombinant Proteins; D012321:DNA-Directed RNA Polymerases