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PMID: 197990 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

RNA phosphorylation: a polynucleotide kinase function in mouse L cell nuclei.

Biochemistry ·Vol. 16 ·No. 19 ·1977-09-20 ·Pages 4233-7

Winicov I

Abstract

Analysis of [gamma-32P]ATP in vitro labeled nuclear RNA shows transfer of gamma-32P from ATP to form the 5'-terminal monophosphate for large RNA molecules. This finding is an actively transcribing nuclear system capable of guanylation and methylation reactions indicates that polynucleotide kinase activity in the eukaryotic nucleus may be functional in kinase reactions involving RNA. It further suggest a participation in the posttranscriptional modification reactions involved in RNA processing. All four nucleosides were found to act as acceptors at the 5' termini of RNA. It is also shown that both ATP and GTP can serve as donors in the nuclear polynucleotide kinase reaction.

MeSH Terms
Adenosine Triphosphate Cell Nucleus/enzymology L Cells/enzymology Molecular Weight Phosphotransferases/metabolism Polynucleotide 5'-Hydroxyl-Kinase/metabolism RNA/metabolism Ribonucleases Ribonucleotides/analysis
Chemicals
Ribonucleotides RNA Adenosine Triphosphate Phosphotransferases Polynucleotide 5'-Hydroxyl-Kinase Ribonucleases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Winicov I
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1977-09-20
Pages
4233-7
Language
English
Region
United States
NLM ID
0370623
Subset
IM
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