2RQP
The Solution Structure of Heterochromatin Protein 1-Binding Protein 74 Histone H1 like domain
Summary for 2RQP
| Entry DOI | 10.2210/pdb2rqp/pdb |
| Descriptor | Heterochromatin protein 1-binding protein 3 (1 entity in total) |
| Functional Keywords | heterochromatin protein 1 binding protein, histone h1, heterochromatin protein 1, alternative splicing, chromosomal protein, dna-binding, nucleus, phosphoprotein, gene regulation |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus (By similarity): Q5SSJ5 |
| Total number of polymer chains | 1 |
| Total formula weight | 9691.54 |
| Authors | Shimamoto, S.,Sugahara, H.,Ohkubo, T. (deposition date: 2009-09-04, release date: 2009-12-29, Last modification date: 2024-05-29) |
| Primary citation | Hayashihara, K.,Uchiyama, S.,Shimamoto, S.,Kobayashi, S.,Tomschik, M.,Wakamatsu, H.,No, D.,Sugahara, H.,Hori, N.,Noda, M.,Ohkubo, T.,Zlatanova, J.,Matsunaga, S.,Fukui, K. The middle region of an HP1-binding protein, HP1-BP74, associates with linker DNA at the entry/exit site of nucleosomal DNA J.Biol.Chem., 285:6498-6507, 2010 Cited by PubMed Abstract: In higher eukaryotic cells, DNA molecules are present as chromatin fibers, complexes of DNA with various types of proteins; chromatin fibers are highly condensed in metaphase chromosomes during mitosis. Although the formation of the metaphase chromosome structure is essential for the equal segregation of replicated chromosomal DNA into the daughter cells, the mechanism involved in the organization of metaphase chromosomes is poorly understood. To identify proteins involved in the formation and/or maintenance of metaphase chromosomes, we examined proteins that dissociated from isolated human metaphase chromosomes by 0.4 m NaCl treatment; this treatment led to significant chromosome decondensation, but the structure retained the core histones. One of the proteins identified, HP1-BP74 (heterochromatin protein 1-binding protein 74), composed of 553 amino acid residues, was further characterized. HP1-BP74 middle region (BP74Md), composed of 178 amino acid residues (Lys(97)-Lys(274)), formed a chromatosome-like structure with reconstituted mononucleosomes and protected the linker DNA from micrococcal nuclease digestion by approximately 25 bp. The solution structure determined by NMR revealed that the globular domain (Met(153)-Thr(237)) located within BP74Md possesses a structure similar to that of the globular domain of linker histones, which underlies its nucleosome binding properties. Moreover, we confirmed that BP74Md and full-length HP1-BP74 directly binds to HP1 (heterochromatin protein 1) and identified the exact sites responsible for this interaction. Thus, we discovered that HP1-BP74 directly binds to HP1, and its middle region associates with linker DNA at the entry/exit site of nucleosomal DNA in vitro. PubMed: 20042602DOI: 10.1074/jbc.M109.092833 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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