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Crystallizing the 6S and 8S spliceosomal assembly intermediates: a complex project.

Jann Patrick Pelz1, Hermann Schindelin2, Katharina van Pee1

  • 1Department of Biochemistry, Theodor Boveri Institute, University of Würzburg, Am Hubland, 97074 Würzburg, Germany.

Acta Crystallographica. Section D, Biological Crystallography
|October 13, 2015
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Summary

Small nuclear ribonucleoproteins (snRNPs) are key to pre-mRNA splicing. Researchers determined the crystal structures of 6S and 8S U snRNP assembly intermediates, revealing insights into spliceosome core formation.

Keywords:
SMNSm proteinsU snRNP assemblycontact engineeringpIClnspliceosomal assemblysurface-entropy reduction

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Small nuclear ribonucleoproteins (snRNPs) are essential for pre-mRNA splicing.
  • The spliceosome, crucial for gene expression, comprises U1, U2, U4/6, and U5 snRNPs.
  • Assembly of the snRNP core involves Sm proteins binding to snRNA, requiring PRMT5 and SMN complexes in vivo.

Purpose of the Study:

  • To elucidate the structural mechanisms of U snRNP assembly.
  • To understand the formation of the common RNP core structure.
  • To provide high-resolution structural insights into key spliceosome assembly intermediates.

Main Methods:

  • X-ray crystallography was employed to determine the structures of 6S and 8S U snRNP complexes.
  • Crystallization involved various rescue strategies, including rational crystal-contact optimization and surface-entropy reduction.
  • Structure-based refinement was used, with the 6S structure guiding the refinement of the 8S structure.

Main Results:

  • The crystal structures of two U snRNP assembly intermediates, the 6S and 8S complexes, were determined.
  • The structures reveal the ordered binding of Sm proteins onto the snRNA Sm site.
  • Successful crystallization strategies were developed and applied, enabling structural determination.

Conclusions:

  • The determined structures offer critical insights into the stepwise assembly of the snRNP core.
  • Understanding these assembly intermediates is vital for comprehending spliceosome biogenesis and function.
  • These findings contribute to the structural understanding of a fundamental cellular process.