RAC protein directs the complete removal of the 3′ external transcribed spacer by the Pac1 nuclease

被引:14
作者
Spasov, K [1 ]
Perdomo, LI [1 ]
Evakine, E [1 ]
Nazar, RN [1 ]
机构
[1] Univ Guelph, Dept Mol Biol & Genet, Guelph, ON N1G 2W1, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
D O I
10.1016/S1097-2765(02)00461-6
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
In Schizosaccharomyces pombe, interdependency in rRNA processing is mediated by a large protein complex (RAC) which contains independent binding sites for each of the transcribed spacers. The RAC complex exhibits no nuclease activity but dramatically alters the efficiency and specificity of the Pac1 nuclease, leading to the complete removal of the 3'ETS. Furthermore, the affinity of RAC protein for mutant 3'ETS correlates closely with in vivo effects on rRNA processing, and changes which disrupt RAC protein binding also inhibit Pac1 nuclease cleavage at the 3' end of the 25S rRNA sequence. The observations indicate that, in the presence of the RAC protein/3'ETS complex, cleavage by the RNase III-like homolog is not restricted to the known intermediate sites but also is directed at the 3' end of the 25S rRNA.
引用
收藏
页码:433 / 437
页数:5
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