Mechanism of Action of Ribonuclease H Isolated from Avian Myeloblastosis Virus and Escherichia coli*
AUTOR(ES)
Leis, Jonathan P.
RESUMO
Purified preparations of RNA-dependent DNA polymerase isolated from avain myeloblastosis virus contain RNase H activity. Labeled ribohomopolymers are degraded in the presence of their complementary deoxyribopolymer, except [3H]poly(U)·poly(dA). The degradation products formed from [3H]poly(A)·poly(dT) were identified as oligonucleotides containing 3′-hydroxyl and 5′-phosphate termini, while AMP was not detected. The nuclease has been characterized as a processive exonuclease that requires ends of poly(A) chains for activity. Exonucleolytic attack occurs in both 5′ to 3′ and 3′ to 5′ directions.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433284Documentos Relacionados
- Mechanistic Independence of Avian Myeloblastosis Virus DNA Polymerase and Ribonuclease H
- A single subunit from avian myeloblastosis virus with both RNA-directed DNA polymerase and ribonuclease H activity
- A Single Subunit from Avian Myeloblastosis Virus with Both RNA-Directed DNA Polymerase and Ribonuclease H Activity
- Mechanism of interaction of avian myeloblastosis virus reverse transcriptase with avian myeloblastosis virus RNA.
- Mechanism of RNA primer removal by the RNase H activity of avian myeloblastosis virus reverse transcriptase.
