期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 384, 期 5, 页码 1262-1272出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.10.001
关键词
histories H1 and H5; HMGB1; intrinsically disordered regions; NMR spectroscopy; protein cross-linking
资金
- Biotechnology and Biological Sciences Research Council [BB/D002257/1]
- Medical Research Council [G0401547]
- BBSRC [BB/E013228/1] Funding Source: UKRI
- MRC [G0401547] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E013228/1, BB/D002257/1] Funding Source: researchfish
- Medical Research Council [G0401547] Funding Source: researchfish
H1 and HMGB1 bind to linker DNA in chromatin, in the vicinity of the nucleosome dyad. They appear to have opposing effects on the nucleosome, H1 stabilising it by sealing two turns of DNA around the octamer, and HMGB1 destabilising it, probably by bending the adjacent DNA. Their presence in chromatin might be mutually exclusive. Displacement/replacement of one by the other as a result of their highly dynamic binding in vivo might, in principle, involve interactions between them. Chemical cross-linking and gel-filtration show that a 1:1 linker histone/HMGB1 complex is formed, which persists at physiological ionic strength, and that complex formation requires the acidic tail of HMGB1. NMR spectroscopy shows that the linker histone binds, predominantly through its basic C-terminal domain, to the acidic tail of HMGB1., thereby disrupting the interaction of the tail with the DNA-binding faces of the HMG boxes. A potential consequence of this interaction is enhanced DNA binding by HMGB1, and concomitantly lowered affinity of H1. for DNA. In a chromatin context, thus might facilitate displacement of H1 by HMGB1. (C) 2008 Elsevier Ltd. All rights reserved.
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