Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Crystal structure of Lsm3 octamer from Saccharomyces cerevisiae: Implications for Lsm ring organisation and recruitment

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Naidoo, N.
  • Harrop, S. J.
  • Sobti, M.
  • Haynes, P. A.
  • Szymczyna, B. R.
  • Williamson, James
  • Curmi, P. M. G.
  • Mabbutt, B. C.

publication date

  • April 2008

journal

  • Journal of Molecular Biology  Journal

abstract

  • Sm and Sm-like (Lsm) proteins are core components of the ribonucleoprotein complexes essential to key nucleic acid processing events within the eukaryotic cell. They assemble as polyprotein ring scaffolds that have the capacity to bind RNA substrates and other necessary protein factors. The crystal structure of yeast Lsm3 reveals a new organisation of the L/Sm beta-propeller ring, containing eight protein subunits. Little distortion of the characteristic L/Sm fold is required to form the octamer, indicating that the eukaryotic Lsm ring may be more pliable than previously thought. The homomeric Lsm3 octamer is found to successfully recruit Lsm6, Lsm2 and Lsm5 directly from yeast lysate. Our crystal structure shows the C-terminal tail of each Lsm3 subunit to be engaged in connections across rings through specific beta-sheet interactions with elongated loops protruding from neighbouring octamers. While these loops are of distinct length for each Lsm protein and generally comprise low-complexity polar sequences, several Lsm C-termini comprise hydrophobic sequences suitable for beta-sheet interactions. The Lsm3 structure thus provides evidence for protein-protein interactions likely utilised by the highly variable Lsm loops and termini in the recruitment of RNA processing factors to mixed Lsm ring scaffolds. Our coordinates also provide updated homology models for the active Lsm[1-7] and Lsm[2-8] heptameric rings.

subject areas

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Dimerization
  • Magnetic Resonance Spectroscopy
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • RNA, Fungal
  • RNA-Binding Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sequence Homology, Amino Acid
scroll to property group menus

Research

keywords

  • RNA processing
  • RNA-binding protein
  • RNP complex
  • Sm-like protein
  • beta-ropeller
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2008.01.007

PubMed ID

  • 18329667
scroll to property group menus

Additional Document Info

start page

  • 1357

end page

  • 1371

volume

  • 377

issue

  • 5

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support