Mechanism of Action of Ribonuclease H Isolated from Avian Myeloblastosis Virus and Escherichia coli | Zendy

Jonathan Leis | Zendy; Ira Berkower | Zendy; Jerard Hurwitz | Zendy

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Mechanism of Action of Ribonuclease H Isolated from Avian Myeloblastosis Virus and Escherichia coli

Author(s) -

Jonathan Leis,

Ira Berkower,

Jerard Hurwitz

Publication year - 1973

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.70.2.466

Subject(s) - nuclease , exonuclease , rnase p , oligonucleotide , rnase h , endonuclease , escherichia coli , ribonuclease , biochemistry , exonuclease iii , dna , dna polymerase i , microbiology and biotechnology , chemistry , polymerase , rna , ribonuclease iii , biology , reverse transcriptase , gene , rna interference

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 [(3)H]poly(U).poly(dA). The degradation products formed from [(3)H]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.RNase H has also been purified from E. coli. This nuclease degrades all homoribopolymers tested in the presence of their complementary deoxyribopolymers to yield oligonucleotides with 5'-phosphate and 3'-hydroxyl termini. E. coli RNase H has been characterized as an endonuclease.

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