Volume 24, No 4, Apr 2014

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 24 Issue 4, April 2014: 497-500   |  Open Access

LETTERS TO THE EDITOR

Crystal structure and biochemical analysis of the heptameric Lsm1-7 complex

Lijun Zhou^1,3,*, Yulin Zhou^1,*, Jing Hang^2,3, Ruixue Wan², Guifeng Lu², Chuangye Yan^2,3 and Yigong Shi^1,3

¹Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
²State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
³Tsinghua-Peking Joint Center for Life Sciences, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China Correspondence: Yigong Shi,(shi-lab@tsinghua.edu.cn)

The Lsm (Sm-like) family of proteins, characterized by the Sm fold1 and conserved among eukaryotes, plays an important role in RNA biogenesis. The Sm and Lsm complexes play an essential role in pre-mRNA splicing2. Of the five small ribonucleoproteins (snRNPs), four (U1, U2, U4, U5) contain the Sm heptamer ring, whereas the U6 snRNP contains a specific Lsm2-8 heptamer that comprises Lsm2, Lsm3, Lsm4, Lsm5, Lsm6, Lsm7, and Lsm83. Another Lsm heptameric complex, Lsm1-7, which differs from Lsm2-8 by one Lsm protein, is thought to function in mRNA decapping, a crucial step in the mRNA degradation pathway4.

10.1038/cr.2014.18

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