Drosophila ribosomal proteins are associated with linker histone H1 and suppress gene transcription

被引:75
作者
Ni, Jian-Quan
Liu, Lu-Ping
Hess, Daniel
Rietdorf, Jens
Sun, Fang-Lin [1 ]
机构
[1] Friedrich Miescher Inst Biomed Res, CH-4058 Basel, Switzerland
[2] Tsinghua Univ, Sch Med, Inst Epigenet & Canc Res, Beijing 100080, Peoples R China
关键词
ribosomal protein; L22; histone H1; chromatin; transcription;
D O I
10.1101/gad.390106
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The dynamics and function of ribosomal proteins in the cell nucleus remain enigmatic. Here we provide evidence that specific components of Drosophila melanogaster ribosomes copurify with linker histone H1. Using various experimental approaches, we demonstrate that this association of nuclear ribosomal proteins with histone H1 is specific, and that colocalization occurs on condensed chromatin in vivo. Chromatin immunoprecipitation analysis confirmed that specific ribosomal proteins are associated with chromatin in a histone H1-dependent manner. Overexpression of either histone H1 or ribosomal protein L22 in Drosophila cells resulted in global suppression of the same set of genes, while depletion of H1 and L22 caused up-regulation of tested genes, suggesting that H1 and ribosomal proteins are essential for transcriptional gene repression. Overall, this study provides evidence for a previously undefined link between ribosomal proteins and chromatin, and suggests a role for this association in transcriptional regulation in higher eukaryotes.
引用
收藏
页码:1959 / 1973
页数:15
相关论文
共 79 条
[1]  
ABMAYR SM, 2003, CURRENT PROTOCOLS PH
[2]  
ALLEN WR, 1978, TRENDS BIOCHEM SCI, V3, pN225
[3]   Nonsense-mediated mRNA decay: terminating erroneous gene expression [J].
Baker, KE ;
Parker, R .
CURRENT OPINION IN CELL BIOLOGY, 2004, 16 (03) :293-299
[4]   Histone H1 is dispensable for methylation-associated gene silencing in Ascobolus immersus and essential for long life span [J].
Barra, JL ;
Rhounim, L ;
Rossignol, JL ;
Faugeron, G .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (01) :61-69
[5]   Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm [J].
Bohnsack, MT ;
Regener, K ;
Schwappach, B ;
Saffrich, R ;
Paraskeva, E ;
Hartmann, E ;
Görlich, D .
EMBO JOURNAL, 2002, 21 (22) :6205-6215
[6]   SPLICING OF XENOPUS-LAEVIS RIBOSOMAL-PROTEIN RNAS IS INHIBITED INVIVO BY ANTISERA TO RIBONUCLEOPROTEINS CONTAINING U1 SMALL NUCLEAR-RNA [J].
BOZZONI, I ;
ANNESI, F ;
BECCARI, E ;
FRAGAPANE, P ;
PIERANDREIAMALDI, P ;
AMALDI, F .
JOURNAL OF MOLECULAR BIOLOGY, 1984, 180 (04) :1173-1178
[7]   Ribosome components are associated with sites of transcription [J].
Brogna, S ;
Sato, TA ;
Rosbash, M .
MOLECULAR CELL, 2002, 10 (01) :93-104
[8]   The dynamics of histone H1 function in chromatin [J].
Bustin, M ;
Catez, F ;
Lim, JH .
MOLECULAR CELL, 2005, 17 (05) :617-620
[9]   Does protein synthesis occur in the nucleus? [J].
Dahlberg, JE ;
Lund, E .
CURRENT OPINION IN CELL BIOLOGY, 2004, 16 (03) :335-338
[10]   Nuclear eukaryotic initiation factor 4E (eIF4E) colocalizes with splicing factors in speckles [J].
Dostie, J ;
Lejbkowicz, F ;
Sonenberg, N .
JOURNAL OF CELL BIOLOGY, 2000, 148 (02) :239-245