Linked Life Data

7237559

Source:http://linkedlifedata.com/resource/pubmed/id/7237559

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-8-20
pubmed:abstractText
The SV40 large T antigen is a multifunctional protein presumed to represent a single translation product of the early viral genes. A wide range of biological controls including the regulation of viral DNA replication, transcription and cell transformation has been attributed to T antigen. Previous evidence has indicated that large T antigen is modified in at least two ways, N-terminal acetylation and amino acid phosphorylation. In this study, we demonstrate a novel modification of a population of SV40 T antigen molecules by poly ADP-ribosylation. The covalent linkage of this oligonucleotide side chain to large T antigen, but not small t antigen, was demonstrated in experiments in which SV40-infected cells were labeled in vivo with 32P-orthophosphate or 14C-adenosine. Treatment of this labeled T antigen with snake venom phosphodiesterase released iso-ADP-ribose or treatment with ADP-ribose glycohydrolase released ADP-ribose. A method has been developed for the in vitro ADP-ribosylation of T antigen present in an infected cell nuclear extract with radiolabeled NAD. Since this type of modification is known to affect enzyme activity, its presence on T antigen suggests a similar role in the regulation of certain biological functions under the control of this protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
567-72
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Modification of SV40 T antigen by poly ADP-ribosylation.
pubmed:publicationType
Journal Article