Conservation of the deadenylase activity of proteins of the Caf1 family in human

被引:82
作者
Bianchin, C
Mauxion, F
Sentis, S
Séraphin, B
Corbo, L
机构
[1] Univ Paris 06, CNRS, UPR2167, Equipe Labellisee Ligue,Ctr Genet Mol, F-91198 Gif Sur Yvette, France
[2] Ctr Leon Berard, INSERM, U590, F-693733 Lyon, France
关键词
Ccr4; mRNA decay; poly(A); Caf1; Pop2; RNase D;
D O I
10.1261/rna.7135305
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
The yeast Pop2 protein, belonging to the eukaryotic Caf1 family, is required for mRNA deadenylation in vivo. it also catalyzes poly(A) degradation in vitro, even though this property has been questioned. Caf1 proteins are related to RNase D, a feature supported by the recently published structure of Pop2. Yeast Pop2 contains, however, a divergent active site while its human homologs harbor consensus catalytic residues. Given these differences, we tested whether its deadenylase activity is conserved in the human homologs Caf1 and Pop2. Our data demonstrate that both human factors degrade poly(A) tails indicating their involvement in mRNA metabolism.
引用
收藏
页码:487 / 494
页数:8
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