Structural Insights into Nuclear pre-mRNA Splicing in Higher Eukaryotes.

Cold Spring Harb Perspect Biol

Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.

Published: November 2019

AI Article Synopsis

  • The spliceosome is a complicated machine made of RNA and proteins that helps cut and rearrange genes in our cells.
  • New technology called cryo-electron microscopy has allowed scientists to see details of how the spliceosome works at a very small level.
  • Even though the way splicing happens is similar in humans and yeast, the human spliceosome is more complex and has different parts compared to yeast.

Article Abstract

The spliceosome is a highly complex, dynamic ribonucleoprotein molecular machine that undergoes numerous structural and compositional rearrangements that lead to the formation of its active site. Recent advances in cyroelectron microscopy (cryo-EM) have provided a plethora of near-atomic structural information about the inner workings of the spliceosome. Aided by previous biochemical, structural, and functional studies, cryo-EM has confirmed or provided a structural basis for most of the prevailing models of spliceosome function, but at the same time allowed novel insights into splicing catalysis and the intriguing dynamics of the spliceosome. The mechanism of pre-mRNA splicing is highly conserved between humans and yeast, but the compositional dynamics and ribonucleoprotein (RNP) remodeling of the human spliceosome are more complex. Here, we summarize recent advances in our understanding of the molecular architecture of the human spliceosome, highlighting differences between the human and yeast splicing machineries.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6824238PMC
http://dx.doi.org/10.1101/cshperspect.a032417DOI Listing

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