共 26 条
A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity
被引:72
作者:

Nakamura, Takahiro
论文数: 0 引用数: 0
h-index: 0
机构:
Nagoya Univ, Ctr Gene Res, Chikusa Ku, Nagoya, Aichi 4648602, Japan
Kyushu Univ, Grad Sch Agr, Fukuoka 8128581, Japan Nagoya Univ, Ctr Gene Res, Chikusa Ku, Nagoya, Aichi 4648602, Japan

Sugita, Mamoru
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h-index: 0
机构:
Nagoya Univ, Ctr Gene Res, Chikusa Ku, Nagoya, Aichi 4648602, Japan Nagoya Univ, Ctr Gene Res, Chikusa Ku, Nagoya, Aichi 4648602, Japan
机构:
[1] Nagoya Univ, Ctr Gene Res, Chikusa Ku, Nagoya, Aichi 4648602, Japan
[2] Kyushu Univ, Grad Sch Agr, Fukuoka 8128581, Japan
来源:
FEBS LETTERS
|
2008年
/
582卷
/
30期
基金:
日本科学技术振兴机构;
日本学术振兴会;
关键词:
PPR protein;
DYW domain;
RNA editing;
Endoribonuclease;
RNase;
D O I:
10.1016/j.febslet.2008.11.017
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:
Many plant pentatricopeptide repeat (PPR) proteins are known to contain a highly conserved C-terminal DYW domain whose function is unknown. Recently, the DYW domain has been proposed to play a role in RNA editing in plant organelles. To address this possibility, we prepared recombinant DYW proteins and tested their cytidine deaminase activity. However, we could not detect any activity in the assays we used. Instead, we found that the recombinant DYW domains possessed endoribonuclease activity and cleaved before adenosine residues in the RNA molecule. Some DYW-containing PPR proteins may catalyze site-specific cleavage of target RNA species. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:4163 / 4168
页数:6
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