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The interaction of the histone H1-related protein phi 0 with chromatin.

作者信息

Olivares C, Azorin F, Subirana J A, Cornudella L

机构信息

Unidad de Quimica Macromolecular del C.S.I.C., Universidad Politecnica de Catalunya, Barcelona, Spain.

出版信息

Biophys Chem. 1987 Oct;28(1):51-7. doi: 10.1016/0301-4622(87)80074-1.

DOI:10.1016/0301-4622(87)80074-1
PMID:3689870
Abstract

Protein phi 0 is a unique protein which is present in the sperm of the sea cucumber, Holothuria tubulosa. It associates with histones, but its physiological role is unknown. From its amino acid composition and sequence, protein phi 0 can be considered as an H1-related protein. In this paper, we have studied its interaction with chicken erythrocyte chromatin particles of different complexity, from core particles to polynucleosomes. Addition of protein phi 0 results in marked chromatin insolubilization. The higher the molecular weight of the chromatin fragment, the lower is the phi 0/nucleosome molar ratio at which precipitation occurs, so that complete insolubilization of polynucleosomes is achieved at a phi 0/nucleosome molar ratio which is identical to that found in mature H. tubulosa spermatozoa. We have also found that the interaction of protein phi 0 with chromatin is cooperative. These findings contribute to clarification of the peculiar physico-chemical properties shown by H. tubulosa sperm chromatin and the role played by the phi 0 protein.

摘要

相似文献

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The interaction of the histone H1-related protein phi 0 with chromatin.
Biophys Chem. 1987 Oct;28(1):51-7. doi: 10.1016/0301-4622(87)80074-1.
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The structure of sea-urchin-sperm histone phi 1 (H1) in chromatin and in free solution. Trypsin digestion and spectroscopic studies.海胆精子组蛋白phi 1(H1)在染色质和游离溶液中的结构。胰蛋白酶消化和光谱学研究。
Eur J Biochem. 1980 Feb;104(1):263-70. doi: 10.1111/j.1432-1033.1980.tb04424.x.

引用本文的文献

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Nucleosomal organization of chromatin in sperm nuclei of the bivalve mollusc Aulacomya ater.双壳贝类软体动物Aulacomya ater精子细胞核中染色质的核小体组织。
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