Structure of a yeast spliceosome at 3.6-angstrom resolution

@article{Yan2015StructureOA,
  title={Structure of a yeast spliceosome at 3.6-angstrom resolution},
  author={Chuangye Yan and Jing Hang and Ruixue Wan and Min Huang and Catherine C L Wong and Yigong Shi},
  journal={Science},
  year={2015},
  volume={349},
  pages={1182 - 1191}
}
Structure and function of the spliceosome When RNA is transcribed from DNA in the eukaryotic cell nucleus, the initial transcript includes noncoding introns that must be spliced out. This splicing is done by a complex macromolecular machine, the spliceosome, which comprises five small nuclear RNAs and more than 100 associated proteins. Now, two papers reveal insights into the structure and function of the yeast spliceosome. Yan et al. describe a high-resolution structure determined by electron… 
Structural basis of pre-mRNA splicing
TLDR
The protein components of the spliceosome anchor both 5′ and 3′ ends of the U2 and U6 snRNAs away from the active site, direct the RNA sequences, and allow sufficient flexibility to deliver RNA components involved in catalyzing the splicing reaction.
Structure of a yeast activated spliceosome at 3.5 Å resolution
TLDR
An atomic structure of an activated spliceosome from Saccharomyces cerevisiae, known as the Bact complex, determined by cryo–electron microscopy at an average resolution of 3.52 angstroms is reported, which outlines a molecular framework for the pre-mRNA splicing reaction.
Structure of a yeast catalytic step I spliceosome at 3.4 Å resolution
TLDR
An atomic structure of a catalytic step I spliceosome from Saccharomyces cerevisiae, as determined by cryo–electron microscopy at an average resolution of 3.4 angstroms is reported, representing the conformation of the splicesome after the first-step reaction.
Molecular Mechanisms of pre-mRNA Splicing through Structural Biology of the Spliceosome.
TLDR
The spliceosome is a protein-directed metalloribozyme, driven by the RNA-dependent ATPase/helicases, resulting in the recruitment and dissociation of specific splicing factors that enable the reaction.
The 3.8 Å structure of the U4/U6.U5 tri-snRNP: Insights into spliceosome assembly and catalysis
TLDR
The three-dimensional structure of a Saccharomyces cerevisiae U4/U6 subcomplex, which comprises the U5 small nuclear ribonucleoprotein (snRNP), the U4 and U6 small nuclear RNA (snRNA) duplex, and a number of protein factors, is determined and reveals the molecular choreography of the snRNAs in the activation process of the spliceosomal ribozyme.
Structural Basis of Nuclear pre-mRNA Splicing: Lessons from Yeast.
TLDR
The structures show how a single RNA catalytic center forms during activation and accomplishes both steps of the splicing reaction, and reveal how spliceosomal helicases remodel thespliceosome for active site formation, substrate docking, reaction product undocking, and splicedosome disassembly.
The Spliceosome: A Protein-Directed Metalloribozyme.
  • Yigong Shi
  • Biology, Medicine
    Journal of molecular biology
  • 2017
TLDR
The spliceosome is proven to be a protein-directed metalloribozyme that maintains the same overall conformation in all structurally characterizedspliceosomes during the splicing reaction.
A Big Bang in spliceosome structural biology
  • J. Cate
  • Biology, Medicine
    Science
  • 2016
TLDR
The first molecular-resolution reconstruction of a central assembly of the human spliceosome, the U4/U6, and structural models of the splicing machinery launch a new era in understanding eukaryotic gene regulation are reported.
The life of U6 small nuclear RNA, from cradle to grave.
TLDR
This review summarizes the current state of knowledge on how U6 snRNA is synthesized, modified, incorporated into snRNPs and spliceosomes, recycled, and degraded.
Structures of the fully assembled Saccharomyces cerevisiae spliceosome before activation
TLDR
Cryo–electron microscopy structures of the pre-B and B complexes reveal the mechanism of assembly and activation for the yeast spliceosome and three B-specific proteins may orient the precursor messenger RNA.
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The protein components of the spliceosome anchor both 5′ and 3′ ends of the U2 and U6 snRNAs away from the active site, direct the RNA sequences, and allow sufficient flexibility to deliver RNA components involved in catalyzing the splicing reaction.
Spliceosome structure and function.
TLDR
The extensive interplay of RNA and proteins in aligning the pre-mRNA's reactive groups, and the presence of both RNA and protein at the core of the splicing machinery, suggest that the spliceosome is an RNP enzyme, but elucidation of the precise nature of its active site awaits the generation of a high-resolution structure of its RNP core.
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TLDR
The structure of U1snRNP provides insights into U1 snRNP assembly and suggests a possible mechanism of 5′-splice-site recognition, a hierarchical network of intricate interactions between subunits.
Structural characterization of the fission yeast U5.U2/U6 spliceosome complex
TLDR
Cryo-electron microscopy is used to produce a 29-Å density map of a stable 37S spliceosomal complex from the genetically tractable fission yeast, Schizosaccharomyces pombe, which closely resembles in vitro purified mammalian C complex.
Crystal structure of Prp8 reveals active site cavity of the spliceosome
TLDR
The crystal structure of yeast Prp8 in complex with Aar2, a U5 small nuclear ribonucleoprotein particle assembly factor, provides crucial insights into the architecture of the spliceosome active site, and reinforces the notion that nuclear pre-mRNA splicing and group II intron splicing have a common origin.
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TLDR
Prp8 is unique, having no obvious homology to other proteins; however, using bioinformatical analysis it is revealed the presence of a conserved RNA recognition motif (RRM), an MPN/JAB domain and a putative nuclear localization signal (NLS).
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TLDR
The data suggest that the U5 snRNP is dramatically remodeled at this stage, with the Prp19 complex and other factors tightly associating, possibly in exchange for other U5 proteins, and suggest that after catalysis the remodeled U5 is eventually released from the postsplicing complex as a 35S snR NP particle.
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TLDR
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TLDR
Using electron microscopy, images of C complex spliceosomes under cryogenic conditions are obtained and a three-dimensional structure of a core complex to a resolution of 30 Å is determined, which reveals a particle of dimensions 27 × 22 × 24 nm with a relatively open arrangement of three primary domains.
Core structure of the U6 small nuclear ribonucleoprotein at 1.7-Å resolution.
TLDR
The crystal structure of the Saccharomyces cerevisiae U 6 snRNP core containing most of the U6 snRNA and all four RRM domains of the Prp24 protein reveals a unique interlocked RNP architecture that sequesters the 5' splice site-binding bases of U6SnRNAs.
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