The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3’-end processing

Aik, Wei Shen; Lin, Min-Han; Tan, Dazhi; Tripathy, Ashutosh; Marzluff, William F.; Dominski, Zbigniew; Chou, Chi-Yuan; Tong, Liang

doi:10.1371/journal.pone.0186034

Title: The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3’-end processing

Journal Article · Wed Oct 11 00:00:00 EDT 2017 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0186034· OSTI ID:1430295

Aik, Wei Shen ^[1]; Lin, Min-Han ^[2]; Tan, Dazhi ^[1]; Tripathy, Ashutosh ^[3]; Marzluff, William F. ^[3]; Dominski, Zbigniew ^[3]; Chou, Chi-Yuan ^[2];

^[1]

Columbia Univ., New York, NY (United States)
National Yang-Ming Univ., Taipei (Taiwan)
Univ. of North Carolina, Chapel Hill, NC (United States)

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.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS); Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS)

Sponsoring Organization:: National Institutes of Health (NIH); Taiwan Ministry of Science and Technology (MOST); • National Institute of General Medical Sciences (NIGMS); Howard Hughes Medical Institute (HHMI); USDOE Office of Science (SC)

Grant/Contract Number:: R35GM118093; S10OD012018; GM29832; 105-2320-B-010-012; 106-2320-B-010-013; S10 RR029205; AC02-06CH11357; AC02-05CH11231

OSTI ID:: 1430295

Journal Information:: PLoS ONE, Vol. 12, Issue 10; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 9 works

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Title: The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3’-end processing

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