ATP-dependent association of nuclear proteins with isolated rat liver nuclei.
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.
Imamoto-Sonobe
N
N
Institute for Molecular and Cellular Biology, Osaka University, Japan.
Yoneda
Y
Y
Iwamoto
R
R
Sugawa
H
H
Uchida
T
T
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002467:Cell Nucleus / Q000378:metabolism*; D005260:Female; D006609:High Mobility Group Proteins / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D056489:Nucleoplasmins; D009865:Oocytes / Q000378:metabolism; D010750:Phosphoproteins; D011485:Protein Binding; D051381:Rats; D013950:Thymus Gland / Q000378:metabolism; D014909:Wheat Germ Agglutinins / Q000494:pharmacology; D014982:Xenopus laevis
D006609:High Mobility Group Proteins; D009687:Nuclear Proteins; D056489:Nucleoplasmins; D010750:Phosphoproteins; D014909:Wheat Germ Agglutinins; D000255:Adenosine Triphosphate