Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription
Retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity. The linkage with the DNA polymerase activity endows the retroviral RNases H with unique properties not found in the cellular counterparts. In addition to the typical endonuclease activity on a DNA/RNA hybrid, cl...
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| Published in | The FEBS journal Vol. 276; no. 6; pp. 1506 - 1516 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
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Oxford, UK
Oxford, UK : Blackwell Publishing Ltd
01.03.2009
Blackwell Publishing Ltd |
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| Abstract | Retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity. The linkage with the DNA polymerase activity endows the retroviral RNases H with unique properties not found in the cellular counterparts. In addition to the typical endonuclease activity on a DNA/RNA hybrid, cleavage by the retroviral enzymes is also directed by both DNA 3' recessed and RNA 5' recessed ends, and by certain nucleotide sequence preferences in the vicinity of the cleavage site. This spectrum of specificities enables retroviral RNases H to carry out a series of cleavage reactions during reverse transcription that degrade the viral RNA genome after minus-strand synthesis, precisely generate the primer for the initiation of plus strands, facilitate the initiation of plus-strand synthesis and remove both plus- and minus-strand primers after they have been extended. |
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| AbstractList | Retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity. The linkage with the DNA polymerase activity endows the retroviral RNases H with unique properties not found in the cellular counterparts. In addition to the typical endonuclease activity on a DNA/RNA hybrid, cleavage by the retroviral enzymes is also directed by both DNA 3′ recessed and RNA 5′ recessed ends, and by certain nucleotide sequence preferences in the vicinity of the cleavage site. This spectrum of specificities enables retroviral RNases H to carry out a series of cleavage reactions during reverse transcription that degrade the viral RNA genome after minus‐strand synthesis, precisely generate the primer for the initiation of plus strands, facilitate the initiation of plus‐strand synthesis and remove both plus‐ and minus‐strand primers after they have been extended. Retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity. The linkage with the DNA polymerase activity endows the retroviral RNases H with unique properties not found in the cellular counterparts. In addition to the typical endonuclease activity on a DNA/RNA hybrid, cleavage by the retroviral enzymes is also directed by both DNA 3' recessed and RNA 5' recessed ends, and by certain nucleotide sequence preferences in the vicinity of the cleavage site. This spectrum of specificities enables retroviral RNases H to carry out a series of cleavage reactions during reverse transcription that degrade the viral RNA genome after minus-strand synthesis, precisely generate the primer for the initiation of plus strands, facilitate the initiation of plus-strand synthesis and remove both plus- and minus-strand primers after they have been extended. [PUBLICATION ABSTRACT] Retroviral reverse transcriptases possess both a DNA polymerase and an RNaseH activity. The linkage with the DNA polymerase activity endows the retroviral RNasesH with unique properties not found in the cellular counterparts. In addition to the typical endonuclease activity on a DNA/RNA hybrid, cleavage by the retroviral enzymes is also directed by both DNA 3'recessed and RNA 5'recessed ends, and by certain nucleotide sequence preferences in the vicinity of the cleavage site. This spectrum of specificities enables retroviral RNasesH to carry out a series of cleavage reactions during reverse transcription that degrade the viral RNA genome after minus-strand synthesis, precisely generate the primer for the initiation of plus strands, facilitate the initiation of plus-strand synthesis and remove both plus- and minus-strand primers after they have been extended. Retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity. The linkage with the DNA polymerase activity endows the retroviral RNases H with unique properties not found in the cellular counterparts. In addition to the typical endonuclease activity on a DNA/RNA hybrid, cleavage by the retroviral enzymes is also directed by both DNA 3' recessed and RNA 5' recessed ends, and by certain nucleotide sequence preferences in the vicinity of the cleavage site. This spectrum of specificities enables the retroviral RNases H to carry out a series of cleavage reactions during reverse transcription to degrade the viral RNA genome after minus strand synthesis, precisely generate the primer for the initiation of plus strands, facilitate the initiation of plus strand synthesis, and remove both plus- and minus-strand primers after they have been extended. |
| Author | Champoux, James J Schultz, Sharon J |
| Author_xml | – sequence: 1 fullname: Champoux, James J – sequence: 2 fullname: Schultz, Sharon J |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19228195$$D View this record in MEDLINE/PubMed |
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| Snippet | Retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity. The linkage with the DNA polymerase activity endows the retroviral... Retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity. The linkage with the DNA polymerase activity endows the retroviral... Retroviral reverse transcriptases possess both a DNA polymerase and an RNaseH activity. The linkage with the DNA polymerase activity endows the retroviral... |
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| SubjectTerms | Biocatalysis Biochemistry catalytic mechanism DNA polymerase DNA/RNA hybrids endonuclease Genomics human immunodeficiency virus, type 1 Models, Molecular Moloney murine leukemia virus Murine leukemia virus polypurine tract Protein Conformation Retroviridae - enzymology reverse transcriptase reverse transcription Ribonuclease H - chemistry Ribonuclease H - metabolism RNA cleavage RNA-directed DNA polymerase RNase H Structure-Activity Relationship Substrate Specificity Substrates Transcription, Genetic Viruses |
| Title | Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription |
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