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

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  • Aik, Wei Shen
    • Other Affiliation: Department of Biological Sciences; Columbia University
  • Lin, Min-Han
    • Other Affiliation: Department of Life Sciences; Institute of Genome Sciences; National Yang-Ming University
  • Tan, Dazhi
    • Other Affiliation: Department of Biological Sciences; Columbia University
  • Tripathy, Ashutosh
    • Affiliation: School of Medicine, Department of Biochemistry and Biophysics
  • Marzluff, William F.
    • Affiliation: School of Medicine, Department of Biochemistry and Biophysics
  • Dominski, Zbigniew
    • Affiliation: School of Medicine, Department of Biochemistry and Biophysics
  • Chou, Chi-Yuan
    • Other Affiliation: Department of Life Sciences; Institute of Genome Sciences; National Yang-Ming University
  • Tong, Liang
    • Other Affiliation: Department of Biological Sciences; Columbia University
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.
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  • Article
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  • In Copyright
Journal title
  • PloS One
Journal volume
  • 12
Journal issue
  • 10
Page start
  • e0186034
Language
  • English
ISSN
  • 1932-6203

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