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	Biophysical and biochemical characterization of recombinant human Pop2 deadenylase
	Liu, Wei-Feng ; Yan, Yong-Bin
	2010-05-11 ; 2010-05-11
关键词	human Pop2 deadenylase divalent metal cation mRNA decay poly(A) tail Ccr4-Not complex MESSENGER-RNA DEADENYLATION POLY(A) TAIL LENGTH POLY(A)-SPECIFIC RIBONUCLEASE POLY(A)-BINDING PROTEIN METHYLENE-BLUE CAF1 PROTEINS RRM DOMAIN YEAST CCR4 IDENTIFICATION Biochemical Research Methods Biochemistry & Molecular Biology Biotechnology & Applied Microbiology
中文摘要	Pop2, a component of the Ccr4-Not complex, functions as a deadenylase both in vitro and in vivo. In this research, we found that the recombinant human Pop2 (hPop2) mainly existed in a compact monomeric state with a alpha + beta tertiary structure type. The percentages of the secondary structures evaluated from the CD spectrum were about 37% alpha-helix, 14% beta-sheet, and 19% beta-turns. The optimal condition for hPop2 catalysis was pH 7-8 at 37 degrees C. Mg2+, Mn2+ and Co2+ had similar effects on the deadenylation activity of hPop2, and the optimal concentration was 0.3-0.5 mM. The deadenylase activity of hPop2 was, at least partially, specific when coordinated with divalent metal ions. The enzyme was not inhibited much by the nucleoticle analogs, and the product 5'-AMP was the most efficient inhibitor. The dissimilarity in the metal ion dependence and inhibitory effects of the nucleoticle analogs suggested that various deadenylases might have differential regulation mechanisms. (c) 2008 Elsevier Inc. All rights reserved.
语种	英语 ; 英语
出版者	ACADEMIC PRESS INC ELSEVIER SCIENCE ; SAN DIEGO ; 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
内容类型	期刊论文
源URL	[http://hdl.handle.net/123456789/26818]
专题	清华大学
推荐引用方式 GB/T 7714	Liu, Wei-Feng,Yan, Yong-Bin. Biophysical and biochemical characterization of recombinant human Pop2 deadenylase[J],2010, 2010.
APA	Liu, Wei-Feng,&Yan, Yong-Bin.(2010).Biophysical and biochemical characterization of recombinant human Pop2 deadenylase..
MLA	Liu, Wei-Feng,et al."Biophysical and biochemical characterization of recombinant human Pop2 deadenylase".(2010).

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