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PMID: 68471 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

tRNATrp (bovine) binding to the reverse transcriptase of avian myeloblastosis virus and function as a heterologous primer.

Baroudy BM, Fournier M, Labouesse J, Papas TS, Chirikjian JG

Abstract

The primary structures for tTNATrp (bovine) and primer tRNATrp (avian) show only minor differences in nucleotide sequence. The heterologous tRNATrp (bovine) appears to have properties similar to the tRNATrp (avian) in its ability to bind the alphabeta from of RNA-dependent DNA nucleotidyltransferase of avian myeloblastosis virus. A stable enzyme-tRNA complex has been isolated by gel filtration. In addition, tRNATrp (bovine) can hydridize to the avian viral 35S RNA and act as a primer for transcription of the RNA. tRNATrp (bovine) can be obtained in larger amounts than the avian primer and can be used to study the interactions between the primer and the viral enzyme.

MeSH Terms
Avian Leukosis Virus/enzymology Avian Myeloblastosis Virus/enzymology DNA, Viral/biosynthesis Nucleic Acid Hybridization Protein Binding RNA, Transfer/isolation & purification,metabolism RNA, Viral/metabolism RNA-Directed DNA Polymerase/metabolism Species Specificity Tryptophan
Chemicals
DNA, Viral RNA, Viral Tryptophan RNA, Transfer RNA-Directed DNA Polymerase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Baroudy B M
Fournier M
Labouesse J
Papas T S
Chirikjian J G
References (32)
32 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1977-05-00
Pages
1889-93
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431037
Subset
IM
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