ArticleJournal of virology2002
Mutations of the RNase H C helix of the Moloney murine leukemia virus reverse transcriptase reveal defects in polypurine tract recognition.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- Insights into Sensing of Murine Retroviruses.Viruses · 2020Review
- Article
- Characterization of interaction between Trim28 and YY1 in silencing proviral DNA of Moloney murine leukemia virus.Virology · 2018Article
- A structure-based mechanism for tRNA and retroviral RNA remodelling during primer annealing.Nature · 2014Article
- Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H.Bioscience reports · 2012Article
- The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding.Retrovirology · 2012Article
- Structural and inhibition studies of the RNase H function of xenotropic murine leukemia virus-related virus reverse transcriptase.Antimicrobial agents and chemotherapy · 2012Article
- Insights into the structure and activity of prototype foamy virus RNase H.Retrovirology · 2012Article
- Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription.The FEBS journal · 2009Review
- RNase H activity: structure, specificity, and function in reverse transcription.Virus research · 2008Review
- Murine leukemia virus reverse transcriptase: structural comparison with HIV-1 reverse transcriptase.Virus research · 2008Review
- Mutational analysis of the N-terminal domain of Moloney murine leukemia virus capsid protein.Journal of virology · 2007Article
- Article
- Purine analog substitution of the HIV-1 polypurine tract primer defines regions controlling initiation of plus-strand DNA synthesis.Nucleic acids research · 2007Article
- Crystal structure of the moloney murine leukemia virus RNase H domain.Journal of virology · 2006Article
- A small loop in the capsid protein of Moloney murine leukemia virus controls assembly of spherical cores.Journal of virology · 2006Article
- Specific recognition and cleavage of the plus-strand primer by reverse transcriptase.Journal of virology · 2005Article
- Effect of polypurine tract (PPT) mutations on human immunodeficiency virus type 1 replication: a virus with a completely randomized PPT retains low infectivity.Journal of virology · 2005Article
- Characterization of the polymerase and RNase H activities of human foamy virus reverse transcriptase.Journal of virology · 2004Article
- Functional characterization of a portion of the Moloney murine leukemia virus gag gene by genetic footprinting.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Both the RNase H domain of Moloney murine leukemia virus (Mo-MLV) reverse transcriptase (RT) and Escherichia coli RNase H possess a positively charged alpha-helix (C helix) and a loop that are not present in the RNase H domains of human immunodeficiency virus (HIV) RT or avian sarcoma virus RT. Although a mutant Mo-MLV RT lacking the C helix (DeltaC RT) retains DNA polymerase activity on homopolymeric substrates and partial RNase H activity, reverse transcription of the viral RNA genome in vivo is defective. To identify the essential features of the C helix, a panel of Mo-MLV RT mutants was generated. Analyses of these mutant viruses revealed the importance of residues H594, I597, R601, and G602. The mutants were tested for their ability to synthesize viral DNA after acute infections and to form proper 5' and 3' viral DNA ends. The mutant RTs were tested in vitro for exogenous RT activity, minus-strand strong-stop DNA synthesis in endogenous RT reactions, nonspecific RNase H activity, and finally, proper cleavage at the polypurine tract-U3 junction. The R601A mutant was the most defective mutant both in vivo and in vitro and possessed very little RNase H activity. The H594A, I597A, and G602A mutants had significant reductions in RNase H activity and in their rates of viral replication. Many of the mutants formed improper viral DNA ends and were less efficient in PPT-U3 recognition and cleavage in vitro. The data show that the C helix plays a crucial role for overall RNase H cleavage activity. The data also suggest that the C helix may play an important role in polypurine tract recognition and proper formation of the plus-strand DNA's 5' end.
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