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PMID: 3844337 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Acylation of adenovirus type 12 early region 1b 18-kDa protein. Further evidence for its localisation in the cell membrane.

FEBS letters ·Vol. 181 ·No. 2 ·1985-02-25 ·Pages 229-35

Grand RJ, Roberts C, Gallimore PH

Abstract

The 18-kDa E1b protein in Ad 12-transformed rat cells and in Ad 12-infected human cells binds lipid strongly. The lipid is not removed by boiling in the presence of SDS or by extraction with methanol/chloroform. It is, however, dissociated from the protein by treatment with methanolic KOH suggesting that attachment is through an ester linkage. The acylated 18-kDa protein is detected only in the membrane fraction. Labelling cell surface proteins on Ad 12-transformed cells with [125I]iodosulphanilic acid shows that some of the Ad 12 18-kDa E1b protein is present on the outside of the cell. It is concluded that this protein is responsible for cell surface T-antigen activity.

MeSH Terms
Acylation Adenoviridae/immunology Animals Antigens, Polyomavirus Transforming Antigens, Viral, Tumor/immunology,metabolism Brain Cell Line Cell Membrane/metabolism Cell Transformation, Viral Embryo, Mammalian Humans Hydroxides/pharmacology Kidney Lipid Metabolism Methanol/pharmacology Palmitic Acid Palmitic Acids/metabolism Potassium/pharmacology Potassium Compounds Rats Tunicamycin/pharmacology Viral Proteins/metabolism
Chemicals
Antigens, Polyomavirus Transforming Antigens, Viral, Tumor Hydroxides Palmitic Acids Potassium Compounds Viral Proteins Tunicamycin Palmitic Acid Potassium potassium hydroxide Methanol
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Grand R J
Roberts C
Gallimore P H
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1985-02-25
Pages
229-35
Language
English
Region
England
NLM ID
0155157
Subset
IM
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