Purification and RNA binding properties of the polycytidylate-binding proteins αCP1 and αCP2

被引：22

作者：

Kiledjian, M ^{[1
]}

Day, N ^{[1
]}

Trifillis, P ^{[1
]}

机构：

[1] Rutgers State Univ, Nelson Biol Labs, Dept Cell Biol & Neurosci, Piscataway, NJ 08854 USA

来源：

METHODS-A COMPANION TO METHODS IN ENZYMOLOGY | 1999年 / 17卷 / 01期

关键词：

D O I：

10.1006/meth.1998.0710

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Regulation of mRNA turnover is a critical control mechanism of gene expression and is influenced by ribonucleoprotein (RNP) complexes that form on cis elements. All mRNAs have an intrinsic half-life and in many cases these half-lives can be altered by a variety of stimuli that are manifested through the formation or disruption of an RNP structure. The stability of alpha-globin mRNA is determined by elements in the 3' untranslated region that are bound by an RNP complex (alpha-complex) which appears to control the erythroid-specific accumulation of alpha-globin mRNA. The alpha-complex could consist of up to six distinct proteins or protein families. One of these families is a prominent polycytidylate binding activity which consists of two highly homologous proteins, alpha-complex proteins 1 and 2 (alpha CP1 and alpha CP2). This article focuses on various methodologies for the detection and manipulation of alpha CP1 and alpha CP2 binding to RNA and details means of isolating and characterizing mRNA bound by these proteins to study mRNA turnover and its regulation. (C) 1999 Academic Press.

引用

页码：84 / 91

页数：8

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