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. 1988 May;85(10):3426–3430. doi: 10.1073/pnas.85.10.3426

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

N Imamoto-Sonobe 1, Y Yoneda 1, R Iwamoto 1, H Sugawa 1, T Uchida 1
PMCID: PMC280224  PMID: 3368451

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.

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Selected References

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