Kazmierczak K M, Davydova E K, Mustaev A A, Rothman-Denes L B
Department of Molecular Genetics and Cell Biology, The University of Chicago, 920 East 58th Street, IL 60637, USA.
EMBO J. 2002 Nov 1;21(21):5815-23. doi: 10.1093/emboj/cdf584.
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.
在体外,噬菌体N4病毒粒子RNA聚合酶(vRNAP)可识别单链模板上体内转录起始位点。N4 vRNAP启动子由一个发夹结构和保守序列组成。在此,我们表明vRNAP由一条含3500个氨基酸的单多肽链组成,并且我们定义并表征了一个具有转录活性的1106个氨基酸的结构域(微型vRNAP)。对该结构域的生化和遗传学表征表明,尽管其启动子特异性独特且与其他依赖DNA的RNA聚合酶缺乏广泛的序列相似性,但微型vRNAP与T7样RNA聚合酶家族相关。