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发表于 2011-12-15 21:53:17
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Evidence that Lin28 stimulates translation by recruiting RNA helicase A to polysomes
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Jianyu Jin1,2,
7 k: a2 p+ P) F8 o4 LWei Jing3,
8 t; S7 h, J+ ^" l' i' m/ j) rXin-Xiang Lei1,2,
+ E, h& w& K8 E( X8 BChen Feng1,4, " T% S" N$ r* ?4 j. q8 p8 Y
Shuping Peng1, ) F# y; J! Q+ P/ M4 |. @) r
Kathleen Boris-Lawrie3 and
1 X. T- ]) D2 v2 A O# b& D2 D, o2 bYingqun Huang1,*
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+ Author Affiliations* S( y9 G& B" T. ?
* r$ Q( l; S' D O# H1Department of Obstetrics, Gynecology and Reproductive Sciences, Yale University School of Medicine, New Haven, CT 06510 USA, 2Department of Chemistry, College of Teacher Education, Wenzhou University, Wenzhou, Zhejiang 325035, China, 3Department of Veterinary Biosciences, Center for RNA Biology, Center for Retrovirus Research, Ohio State University, Columbus, OH 43210 USA and 4Department of Biochemistry and Molecular Biology, China Medical University, Shenyang, Liaoning 110001, China : S6 S3 W' l: H2 a
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*To whom correspondence should be addressed. Tel: +1 203 737 2578; Fax: +1 203 785 7134; Email: yingqun.huang@yale.edu
. }% A) ]0 U$ g1 TReceived November 23, 2010. 4 l3 S6 N7 r* X- e
Revision received December 21, 2010.
4 D" ^+ E9 g$ F" n+ h6 @Accepted December 22, 2010.
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Abstract) Z: Y, k K6 G! k: p" G
- w+ f: K, S* ~2 fThe stem cell protein Lin28 functions to inhibit the biogenesis of a group of miRNAs but also stimulates the expression of a subset of mRNAs at the post-transcriptional level, the underlying mechanism of which is not yet understood. Here we report the characterization of the molecular interplay between Lin28 and RNA helicase A (RHA) known to play an important role in remodeling ribonucleoprotein particles during translation. We show that reducing Lin28 expression results in decreased RHA association with polysomes while increasing Lin28 expression leads to elevated RHA association. Further, the carboxyl terminus of Lin28 is necessary for interaction with both the amino and carboxyl termini of RHA. Importantly, a carboxyl terminal deletion mutant of Lin28 that retains RNA-binding activity fails to interact with RHA and exhibits dominant-negative effects on Lin28-dependent stimulation of translation. Taken together, these results lead us to su ggest that Lin28 may stimulate translation by actively recruiting RHA to polysomes. 1 t$ W* V8 i! w& D
© The Author(s) 2011. Published by Oxford University Press.+ @; n, @- a2 P2 v/ H/ T
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& Y- d6 f, ^1 Y3 ~This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
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