动质体RNA编辑相关蛋白1（REAP-1）：一种具有重复结构域的新型编辑复合蛋白。
Kinetoplastid RNA-editing-associated protein 1 (REAP-1): a novel editing complex protein with repetitive domains.
作者信息
Madison-Antenucci S, Sabatini R S, Pollard V W, Hajduk S L
机构信息
Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
出版信息
EMBO J. 1998 Nov 2;17(21):6368-76. doi: 10.1093/emboj/17.21.6368.
Abstract
Kinetoplastid RNA editing consists of the addition or deletion of uridines at specific sites within mitochondrial mRNAs. This unusual RNA processing event is catalyzed by a ribonucleoprotein (RNP) complex that includes editing site-specific endoribonuclease, RNA ligase and terminal uridylnucleotidyl transferase (Tutase) among its essential enzymatic activities. To identify the components of this RNP, monoclonal antibodies were raised against partially purified editing complexes. One antibody reacts with a mitochondrially located 45 kDa polypeptide (p45) which contains a conserved repetitive amino acid domain. p45 co-purifies with RNA ligase and Tutase in a large ( approximately 700 kDa) RNP, and anti-p45 antibody inhibits in vitro RNA editing. Thus, p45 is the first kinetoplastid RNA-editing-associated protein (REAP-1) that has been cloned and identified as a protein component of a functional editing complex.
摘要
动质体RNA编辑包括在线粒体mRNA的特定位点添加或删除尿苷。这种不同寻常的RNA加工事件由一种核糖核蛋白（RNP）复合体催化，该复合体的基本酶活性包括编辑位点特异性内切核糖核酸酶、RNA连接酶和末端尿苷酰基转移酶（Tutase）。为了鉴定该RNP的组成成分，制备了针对部分纯化的编辑复合体的单克隆抗体。一种抗体与位于线粒体的45 kDa多肽（p45）发生反应，该多肽含有一个保守的重复氨基酸结构域。p45在一个大型（约700 kDa）RNP中与RNA连接酶和Tutase共同纯化，并且抗p45抗体在体外抑制RNA编辑。因此，p45是第一个被克隆并鉴定为功能性编辑复合体蛋白质成分的动质体RNA编辑相关蛋白（REAP-1）。
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