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PMID: 2522559 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Ability of p53 and the adenovirus E1b 58-kilodalton protein to form a complex is determined by p53.

Journal of virology ·Vol. 63 ·No. 4 ·1989-04-00 ·Pages 1792-9

Braithwaite AW, Jenkins JR

Abstract

We have investigated p53-E1b 58-kilodalton (kDa) protein complex formation during permissive and semipermissive infections with adenovirus type 5 (Ad5) dl309. While metabolic labeling studies easily detected p53-E1b 58-kDa protein complexes in transformed rat cells (XhoI-C), the same methods have not revealed complexes during infection of either human osteosarcoma cells (permissive) or normal rat kidney cells (semipermissive). Complexes were not detectable at any stage during the replicative cycle of Ad5 dl309 in osteosarcoma cells, and they could not be stabilized by using an in vivo cross-linking agent. In addition, using the E4-defective mutant Ad5 dl355, no complexes were observed either. Thus, the lack of p53-E1b 58-kDa protein complex formation during infection is not due to competition from the E4 34-kDa protein. In vitro association experiments showed that in vitro-translated mouse and human p53 could form complexes with E1b 58-kDa antigen expressed during infection. Thus, such E1b proteins are competent to form complexes. The converse experiment, in which in vitro-translated E1b 58-kDa protein was mixed with lysates of osteosarcoma cells, showed little or no p53-E1b 58-kDa protein association, even though the in vitro E1b 58-kDa protein could associate stably with p53 from cells containing endogenous p53-E1b 58-kDa protein complex. These data suggest that competence to form p53-E1b 58-kDa protein complexes resides in some property of p53.

MeSH Terms
Adenovirus Early Proteins Adenoviruses, Human/genetics Animals Cell Transformation, Viral Cells, Cultured Humans Macromolecular Substances Mice Molecular Weight Neoplasm Proteins/physiology Oncogene Proteins, Viral/physiology Phosphoproteins/physiology Rats Structure-Activity Relationship Tumor Suppressor Protein p53 Virus Replication
Chemicals
Adenovirus Early Proteins Macromolecular Substances Neoplasm Proteins Oncogene Proteins, Viral Phosphoproteins Tumor Suppressor Protein p53
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Braithwaite A W
Marie Curie Research Institute, Oxted, Surrey, England.
Jenkins J R
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.63.4.1792-1799.1989
Published
1989-04-00
Pages
1792-9
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC248446
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.63.4.1792-1799.1989 PMC Full Text View journal details
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