Poly(A) RNA and Paip2 act as allosteric regulators of poly(A)-binding protein

  • Lee, Seung Hwan; 
  • Oh, Jungsic; 
  • Park, Jonghyun; 
  • Paek, Ki Young; 
  • Rho, Sangchul; 
  • 외 2명
Citations

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초록

When bound to the 30 poly(A) tail of mRNA, poly(A)binding protein (PABP) modulates mRNA translation and stability through its association with various proteins. By visualizing individual PABP molecules in real time, we found that PABP, containing four RNA recognition motifs (RRMs), adopts a conformation on poly(A) binding in which RRM1 is in proximity to RRM4. This conformational change is due to the bending of the region between RRM2 and RRM3. PABP-interacting protein 2 actively disrupts the bent structure of PABP to the extended structure, resulting in the inhibition of PABP-poly(A) binding. These results suggest that the changes in the configuration of PABP induced by interactions with various effector molecules, such as poly(A) and PABP-interacting protein 2, play pivotal roles in its function.

키워드

EUKARYOTIC TRANSLATION INITIATION; POLYADENYLATE-BINDING PROTEIN; MESSENGER-RNA; CYTOPLASMIC POLY(A)-RIBONUCLEOPROTEIN; REPEATING STRUCTURE; STRUCTURAL BASIS; DOMAIN; RECOGNITION; REPRESSION; PABP
제목
Poly(A) RNA and Paip2 act as allosteric regulators of poly(A)-binding protein
저자
Lee, Seung Hwan; Oh, Jungsic; Park, Jonghyun; Paek, Ki Young; Rho, Sangchul; Jang, Sung Key; Lee, Jong-Bong
DOI
10.1093/nar/gkt1170
발행일
2014-02
유형
Article
저널명
Nucleic Acids Research
권
42
호
4
페이지
2697 ~ 2707

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