The N-terminal Domains of FLASH and Lsm11 Form a 2:1 Heterotrimer for Histone Pre-mRNA 3'-end Processing

Overview

Journal PLoS One

Specialties General Medicine
Science

Date 2017 Oct 12

PMID 29020104

Citations 11

Authors

Wei Shen Aik

Min-Han Lin

Dazhi Tan

Ashutosh Tripathy

William F Marzluff

Zbigniew Dominski

Chi-Yuan Chou

Liang Tong

Affiliations

Soon will be listed here.

Abstract

Unlike canonical pre-mRNAs, animal replication-dependent histone pre-mRNAs lack introns and are processed at the 3'-end by a mechanism distinct from cleavage and polyadenylation. They have a 3' stem loop and histone downstream element (HDE) that are recognized by stem-loop binding protein (SLBP) and U7 snRNP, respectively. The N-terminal domain (NTD) of Lsm11, a component of U7 snRNP, interacts with FLASH NTD and these two proteins recruit the histone cleavage complex containing the CPSF-73 endonuclease for the cleavage reaction. Here, we determined crystal structures of FLASH NTD and found that it forms a coiled-coil dimer. Using solution light scattering, we characterized the stoichiometry of the FLASH NTD-Lsm11 NTD complex and found that it is a 2:1 heterotrimer, which is supported by observations from analytical ultracentrifugation and crosslinking.

Citing Articles

In vitro methylation of the U7 snRNP subunits Lsm11 and SmE by the PRMT5/MEP50/pICln methylosome.

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Spatiotemporal higher-order chromatin landscape of human histone gene clusters at histone locus bodies during the cell cycle in breast cancer progression.

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