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Allosteric regulation of human poly(A)-specific ribonuclease by cap and potassium ions
Liu, Wei-Feng ; Zhang, Ao ; Cheng, Yuan ; Zhou, Hai-Meng ; Yan, Yong-Bin
2010-10-12 ; 2010-10-12
关键词Poly(A)-specific ribonuclease (PARN) Allosteric regulation Deadenylase The cap structure mRNA decay MESSENGER-RNA DEADENYLATION RRM DOMAIN POLY(A) BINDING PARN STABILITY SITE RECOGNITION EXONUCLEASE TURNOVER REMOVAL Biochemistry & Molecular Biology Biophysics
中文摘要Poly(A)-specific ribonuclease (PARN), a multi-domain dimeric enzyme, is a deadenylase in higher vertebrates and plants with the unique property of cap-dependent catalysis and processivity. We found that PARN is an allosteric enzyme, and potassium ions and the cap analogue were effectors with binding sites located at the RRM domain. The binding of K+ to the entire RRM domain led to an increase of substrate-binding affinity but a decrease in the cooperativity of the substrate-binding site, while the binding of the cap analogue decreased both the catalytic efficiency and the substrate-binding affinity. The dissimilar kinetic properties of the enzymes with and Without the entire RRM domain Suggested that the RRM domain played a central role in the allosteric communications of PARN regulation. The allostery is proposed to be important to the multi-level regulation of PARN to achieve precise control of the mRNA poly(A) tail length. (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/123456789/81765]  
专题清华大学
推荐引用方式
GB/T 7714
Liu, Wei-Feng,Zhang, Ao,Cheng, Yuan,et al. Allosteric regulation of human poly(A)-specific ribonuclease by cap and potassium ions[J],2010, 2010.
APA Liu, Wei-Feng,Zhang, Ao,Cheng, Yuan,Zhou, Hai-Meng,&Yan, Yong-Bin.(2010).Allosteric regulation of human poly(A)-specific ribonuclease by cap and potassium ions..
MLA Liu, Wei-Feng,et al."Allosteric regulation of human poly(A)-specific ribonuclease by cap and potassium ions".(2010).
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