Histone H1 diversity: bridging regulatory signals to linker histone function

被引:103
作者
Khochbin, S [1 ]
机构
[1] Inst Albert Bonniot, Fac Med, INSERM U309,Lab Biol Mol & Cellulaire Differencia, Equipe Chromatine & Express Genes, F-38706 La Tronche, France
关键词
transcription; acetylation; methylation; remodeling; differentiation;
D O I
10.1016/S0378-1119(01)00495-4
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Genes encoding linker histone variants have evolved to link their expression to signals controlling the proliferative capacities of cells, i.e. cycling and growth-arrested cells express distinct and specific HI subtypes. In metazoan, these variants show a tripartite structure, with considerably divergent sequences in their amino and carboxyl. terminus domains. The aim of this review is to show how specific regulatory signals control the expression of an individual H1 and to discuss the functional significance of the two variables associated with a linker histone: its primary sequence and the timing of its expression. (C) 2001 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:1 / 12
页数:12
相关论文
共 105 条
[51]   A HISTONE H-1 PROTEIN IN SEA-URCHINS IS ENCODED BY A POLY(A)+ MESSENGER-RNA [J].
LIEBER, T ;
ANGERER, LM ;
ANGERER, RC ;
CHILDS, G .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1988, 85 (12) :4123-4127
[52]   Normal spermatogenesis in mice lacking the testis-specific linker histone H1t [J].
Lin, QC ;
Sirotkin, A ;
Skoultchi, AI .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (06) :2122-2128
[53]   The five cleavage-stage (CS) histones of the sea urchin are encoded by a maternally expressed family of replacement histone genes: Functional equivalence of the CS H1 and frog H1M (B4) proteins [J].
Mandl, B ;
Brandt, WF ;
SupertiFurga, G ;
Graninger, PG ;
Birnstiel, ML ;
Busslinger, M .
MOLECULAR AND CELLULAR BIOLOGY, 1997, 17 (03) :1189-1200
[54]   H1TF2A, THE LARGE SUBUNIT OF A HETERODIMERIC, GLUTAMINE-RICH CCAAT-BINDING TRANSCRIPTION FACTOR INVOLVED IN HISTONE H1 CELL-CYCLE REGULATION [J].
MARTINELLI, R ;
HEINTZ, N .
MOLECULAR AND CELLULAR BIOLOGY, 1994, 14 (12) :8322-8332
[55]   Conserved sequence elements in human main type-H1 histone gene promoters:: their role in H1 gene expression [J].
Meergans, T ;
Albig, W ;
Doenecke, D .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1998, 256 (02) :436-446
[56]  
MEISTRICH ML, 1989, HISTONE OTHER BASIC
[57]   HISTONES OF RAINBOW-TROUT ERYTHROCYTES INCLUDE AN ERYTHROCYTE-SPECIFIC HISTONE [J].
MIKI, BLA ;
NEELIN, JM .
CANADIAN JOURNAL OF BIOCHEMISTRY, 1975, 53 (11) :1158-1169
[58]   Dynamic binding of histone H1 to chromatin in living cells [J].
Misteli, T ;
Gunjan, A ;
Hock, R ;
Bustin, M ;
Brown, DT .
NATURE, 2000, 408 (6814) :877-881
[59]   THE HISTONE H1-DEGREES/H5 VARIANT AND TERMINAL DIFFERENTIATION OF CELLS DURING DEVELOPMENT OF XENOPUS-LAEVIS [J].
MOORMAN, AFM ;
DEBOER, PAJ ;
CHARLES, R ;
LAMERS, WH .
DIFFERENTIATION, 1987, 35 (02) :100-107
[60]   PIPPin is a brain-specific protein that contains a cold-shock domain and binds specifically to H1° and H3.3 mRNAs [J].
Nastasi, T ;
Scaturro, M ;
Bellafiore, M ;
Raimondi, L ;
Beccari, S ;
Cestelli, A ;
Di Liegro, I .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (34) :24087-24093