The Sea Urchin Sperm Histone H2B Readily Forms a Complex with Heterologous H2A Despite Having an Elongated N-Terminal Domain
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چکیده
منابع مشابه
Evolution of late H2A, H2B, and H4 histone genes of the sea urchin, Strongylocentrotus purpuratus.
Sea urchins possess several distinct sets of histone genes, including "early" genes, maximally active in cleavage and blastula stages, and "late" genes, active from the late blastula stage onwards. We determined the nucleotide sequences of six sea urchin (Strongylocentrotus purpuratus) late histone genes located on four genomic segments. Comparative analysis of these sequences identified severa...
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Histone ubiquitylation has emerged as an important chromatin modification with roles in transcription and trans-histone methylation. In the past several years, there has been dramatic progress in the identification of factors that control ubiquitin attachment to the core histones H2A and H2B. Recent advances in this area will be reviewed, and outstanding questions relating to the cellular funct...
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The late histone genes of the sea urchin Psarnnechinus miliaris can be classified as strictly embryonic, tissue-specific or somatic according to their expression in adult tissues (1). We have isolated a member of the H2B-1 gene family that differs from a late H2B-1 cDNA (2) by 7% nucleotide substitution (not shown).. The expression pattern of this gene is somatic, as its mRNA (like the other cr...
متن کاملSolution structure of the isolated histone H2A-H2B heterodimer
During chromatin-regulated processes, the histone H2A-H2B heterodimer functions dynamically in and out of the nucleosome. Although detailed crystal structures of nucleosomes have been established, that of the isolated full-length H2A-H2B heterodimer has remained elusive. Here, we have determined the solution structure of human H2A-H2B by NMR coupled with CS-Rosetta. H2A and H2B each contain a h...
متن کاملThe histone H3/H4.N1 complex supplemented with histone H2A-H2B dimers and DNA topoisomerase I forms nucleosomes on circular DNA under physiological conditions.
We have fractionated the whole cell extract of Xenopus oocytes (oocyte S-150) and isolated the endogenous components required for DNA supercoiling and nucleosome formation. Histone H2B and the three oocyte-specific H2A proteins were purified as free histones. Histones H3 and H4 were purified 100-fold in a complex with the acidic protein N1. In the presence of DNA topoisomerase I or II, histone ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1981
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1981.tb05190.x