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PMID: 3368451 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

ATP-dependent association of nuclear proteins with isolated rat liver nuclei.

Imamoto-Sonobe N, Yoneda Y, Iwamoto R, Sugawa H, Uchida T

Abstract

In vitro association of Xenopus nucleoplasmin and mammalian nonhistone chromosomal high mobility group 1 (HMG1) protein with nuclei isolated from rat liver was examined. Efficient association of nuclear proteins with isolated nuclei requires ATP, HCO3-, and Ca2+. Association occurred at 33 degrees C but not at 4 degrees C. ATP could be replaced by adenosine 5'-[alpha,beta-methylene]triphosphate (pp[CH2]pA), a nonhydrolyzable ATP analog. pp[CH2]pA associated with nuclei at 33 degrees C and nucleoplasmin and HMG1 rapidly associated with the pp[CH2]pA-bound nuclei at 4 degrees C. Competition studies showed that these associations at both 33 degrees C and 4 degrees C were specific. More than 80% of the bindings of nuclear proteins to the nuclear surface were blocked by wheat germ agglutinin.

MeSH Terms
Adenosine Triphosphate/metabolism Animals Cattle Cell Nucleus/metabolism Female High Mobility Group Proteins/metabolism Kinetics Liver/metabolism Nuclear Proteins/metabolism Nucleoplasmins Oocytes/metabolism Phosphoproteins Protein Binding Rats Thymus Gland/metabolism Wheat Germ Agglutinins/pharmacology Xenopus laevis
Chemicals
High Mobility Group Proteins Nuclear Proteins Nucleoplasmins Phosphoproteins Wheat Germ Agglutinins Adenosine Triphosphate
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Imamoto-Sonobe N
Institute for Molecular and Cellular Biology, Osaka University, Japan.
Yoneda Y
Iwamoto R
Sugawa H
Uchida T
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1988-05-00
Pages
3426-30
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC280224
Subset
IM
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