RNase H domain mutations affect the interaction between Moloney murine leukemia virus reverse transcriptase and its primer-template.
RNase H domain mutations affect the interaction between Moloney murine leukemia virus reverse transcriptase and its primer-template.
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RNase H 结构域突变影响莫洛尼鼠白血病病毒逆转录酶与其引物模板之间的相互作用。
DOI：
10.1073/pnas.90.4.1276
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发表时间：
1993
影响因子：
11.1
通讯作者：
Goff,SP
中科院分区：
文献类型：
--
作者：
Telesnitsky,A;Goff,SP
The active sites for the polymerase and nuclease activities of Moloney murine leukemia virus (M-MuLV) reverse transcriptase (RT) reside in separate domains of a single polypeptide. We have studied the effects of RNase H domain mutations on DNA polymerase activity. These mutant RTs displayed decreased processivity of DNA synthesis. We also compared complexes formed between primer-templates and mutant and wild-type reverse transcriptase (RT). Although M-MuLV RT is monomeric in solution, two molecules of RT bound DNA cooperatively, suggesting that M-MuLV RT binds primer-template as a dimer. Some mutant RTs with decreased processivity failed to form the putative dimer.
