RNase H domain mutations affect the interaction between Moloney murine leukemia virus reverse transcriptase and its primer-template. | Zendy

Alice Telesnitsky | Zendy; S P Goff | Zendy

Open Access

RNase H domain mutations affect the interaction between Moloney murine leukemia virus reverse transcriptase and its primer-template.

Author(s) -

Alice Telesnitsky,

S P Goff

Publication year - 1993

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.90.4.1276

Subject(s) - reverse transcriptase , processivity , primer (cosmetics) , murine leukemia virus , dna polymerase , rnase h , microbiology and biotechnology , biology , polymerase , mutant , dna , rna directed dna polymerase , nuclease , virology , chemistry , virus , polymerase chain reaction , biochemistry , gene , organic chemistry

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.

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