Literature DB >> 12644557

Sequence complexity of histone H1 subtypes.

Imma Ponte1, Roger Vila, Pedro Suau.   

Abstract

H1 subtypes are involved in chromatin higher-order structure and gene regulation. H1 has a characteristic three-domain structure. We studied the length variation of the available H1 subtypes and showed that the length of the N-terminal and C-terminal domains was more variable than that of the central domain. The N-terminal and C-terminal domains were of low sequence complexity both at the nucleotide and at the amino acid level, whereas the globular domain was of high complexity. In most subtypes, low complexity was due only to cryptic simplicity, which reflects the clustering of a number of short and often imperfect sequence motifs. However, a subset of subtypes from eubacteria, plants, and invertebrates contained tandem repeats of short amino acid motifs (four to 12 residues), which could amount to a large proportion of the terminal domains. In addition, some other subtypes, such as those of Drosophila and mammalian H1t, were only marginally simple. The coexistence of these three kinds of subtypes suggests that the terminal domains could have originated in the amplification of short sequence motifs, which would then have evolved by point mutation and further slippage.

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Year:  2003        PMID: 12644557     DOI: 10.1093/molbev/msg041

Source DB:  PubMed          Journal:  Mol Biol Evol        ISSN: 0737-4038            Impact factor:   16.240


  15 in total

1.  Isolation and characterization of a novel H1.2 complex that acts as a repressor of p53-mediated transcription.

Authors:  Kyunghwan Kim; Jongkyu Choi; Kyu Heo; Hyunjung Kim; David Levens; Kimitoshi Kohno; Edward M Johnson; Hugh W Brock; Woojin An
Journal:  J Biol Chem       Date:  2008-02-07       Impact factor: 5.157

2.  Polymorphism in a histone H1 subtype with a short N-terminal domain in three legume species (Fabaceae, Fabaeae).

Authors:  Oleg E Kosterin; Vera S Bogdanova; Andrey A Kechin; Olga O Zaytseva; Arseniy K Yadrikhinskiy
Journal:  Mol Biol Rep       Date:  2012-10-11       Impact factor: 2.316

Review 3.  Yeast HMO1: Linker Histone Reinvented.

Authors:  Arvind Panday; Anne Grove
Journal:  Microbiol Mol Biol Rev       Date:  2016-11-30       Impact factor: 11.056

4.  Evolution of the regular zone of histone H1 in fabaceae plants.

Authors:  Yuri Trusov; Vera S Bogdanova; Vladimir A Berdnikov
Journal:  J Mol Evol       Date:  2004-10       Impact factor: 2.395

Review 5.  Structure of the H1 C-terminal domain and function in chromatin condensation.

Authors:  Tamara L Caterino; Jeffrey J Hayes
Journal:  Biochem Cell Biol       Date:  2011-02       Impact factor: 3.626

Review 6.  Histone variants: The unsung guardians of the genome.

Authors:  Ernest O N Phillips; Akash Gunjan
Journal:  DNA Repair (Amst)       Date:  2022-02-17

7.  Linker Histone H1.2 cooperates with Cul4A and PAF1 to drive H4K31 ubiquitylation-mediated transactivation.

Authors:  Kyunghwan Kim; Bomi Lee; Jaehoon Kim; Jongkyu Choi; Jin-Man Kim; Yue Xiong; Robert G Roeder; Woojin An
Journal:  Cell Rep       Date:  2013-12-19       Impact factor: 9.423

8.  Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1.

Authors:  Alicia Roque; Inma Ponte; Pedro Suau
Journal:  Biophys J       Date:  2007-05-18       Impact factor: 4.033

Review 9.  Classification of intrinsically disordered regions and proteins.

Authors:  Robin van der Lee; Marija Buljan; Benjamin Lang; Robert J Weatheritt; Gary W Daughdrill; A Keith Dunker; Monika Fuxreiter; Julian Gough; Joerg Gsponer; David T Jones; Philip M Kim; Richard W Kriwacki; Christopher J Oldfield; Rohit V Pappu; Peter Tompa; Vladimir N Uversky; Peter E Wright; M Madan Babu
Journal:  Chem Rev       Date:  2014-04-29       Impact factor: 60.622

10.  Fine mapping of posttranslational modifications of the linker histone H1 from Drosophila melanogaster.

Authors:  Ana Villar-Garea; Axel Imhof
Journal:  PLoS One       Date:  2008-02-06       Impact factor: 3.240

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