A yeast homolog of chromatin assembly factor 1 is involved in early ribosome assembly

被引:38
作者
Schaper, S
Fromont-Racine, M
Linder, P
de la Cruz, J
Namane, A
Yaniv, M
机构
[1] Inst Pasteur, Dept Biochim & Genet Mol, Lab Chim Struct Macromol, URA 2185 CNRS, F-75724 Paris 15, France
[2] Univ Geneva, Ctr Med Univ, Dept Biochim Med, CH-2111 Geneva, Switzerland
[3] Inst Pasteur, Dept Biotechnol, Unite Genet Interact Macromol, F-75724 Paris 15, France
[4] Inst Pasteur, Dept Biotechnol, URA 1644 CNRS, Unite Virus Oncogenes, F-75724 Paris 15, France
关键词
D O I
10.1016/S0960-9822(01)00584-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cells have a recurrent need for the correct assembly of protein-nucleic acid complexes. We have studied a yeast homolog of the smallest subunit of chromatin assembly factor 1 (CAM), encoded by YMR131c and termed "RRB1" [1]. Unlike other yeast homologs, Msi1p, and Hat2p, Rrb1p is essential for cell viability. Impairment of Rrb1p function results in decreased levels of free 60S ribosomal subunits and the appearance of half-mer polysomes, suggesting its involvement in ribosome biogenesis. Using tandem affinity purification (TAP [2]) combined with mass spectrometry, we show that Rrb1p is associated with ribosomal protein L3. A fraction of Rrb1p is also found in a protein-precursor rRNA complex containing at least ten other early-assembling ribosomal proteins. We propose that Rrb1p is required for proper assembly of preribosomal particles during early ribosome biogenesis, presumably by targeting L3 onto the 35S precursor rRNA. This action may resemble the mechanism by which CAM assembles histones H3/H4 onto newly replicated DNA.
引用
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页码:1885 / 1890
页数:6
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