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Journal of Biochemistry Advance Access originally published online on January 30, 2008
Journal of Biochemistry 2008 143(3):287-293; doi:10.1093/jb/mvn013
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© 2008 The Japanese Biochemical Society.

JB Minireviews-Functional Dynamics of the Nucleus

Cracking the Enigmatic Linker Histone Code

James S. Godde1,2 and Kiyoe Ura1,*

1Division of Gene Therapy Science, Osaka University Graduate School of Medicine, 2-2 Yamada-oka, Suita, Osaka 565-0871, Japan; and 2Department of Biology, Monmouth College, 700 East Broadway, Monmouth, IL 61462 USA

*To whom correspondence should be addressed. Tel: +81 6 6879 3901, Fax: +81 6 6879 3909, E-mail: kiyoeura{at}gts.med.osaka-u.ac.jp

Received November 16, 2007; Accepted December 1, 2007


  Abstract

Recently, the existence of a ‘histone code’ has been proposed to explain the link between the covalent chemical modification of histone proteins and the epigenetic regulation of gene activity. Although the role of the four ‘core’ histones has been extensively studied, little is known about the involvement of the linker histone, histone H1 and its variants, in this code. For many years, few sites of chemical modification had been mapped in linker histones, but this has changed recently with the use of functional proteomic techniques, principally mass spectrometry, to characterize these modifications. The functionality of many of these sites, however, remains to be determined.

Key Words: epigenetic code, histone H1, histone modification, histone variant, linker histone

Abbreviations: bp, base pairs; CHO, Chinese Hamster Ovary; ES, embryonic stem; HPLC, High Performance Liquid Chromatography; Rb, retinoblastoma protein


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