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PMID: 3044369 Published · ppublish English Journal Article

Acetylated HMG1 protein interacts specifically with homologous DNA polymerase alpha in vitro.

Biochemical and biophysical research communications ·Vol. 154 ·No. 3 ·1988-08-15 ·Pages 918-27

Alexandrova EA, Beltchev BG

Abstract

The acetylated, deacetylated and nonacetylated forms of HMG1 proteins from Guerin ascites tumour cells and calf thymus were separated and their in vitro interactions with homologous and heterologous DNA polymerases were studied. It has been found that only the acetylated form of HMG1 proteins forms a specific complex with homologous DNA polymerase alpha and stimulates its activity in vitro. The acetylation therefore is necessary for their possible function in DNA replication. This finding represents an evidence for a relationship between the acetylation of HMG1 proteins and their biological role.

MeSH Terms
Acetylation Animals DNA Polymerase II/metabolism Escherichia coli/enzymology High Mobility Group Proteins/isolation & purification,metabolism Kinetics Neoplasms, Experimental/enzymology Osmolar Concentration Protein Binding Rats Thymus Gland/metabolism
Chemicals
High Mobility Group Proteins DNA Polymerase II
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Alexandrova E A
Institute of Molecular Biology, Bulgarian Academy of Sciences, Sofia.
Beltchev B G
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1988-08-15
Pages
918-27
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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