Results 271 to 280 of about 10,182 (283)
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A glimpse into the spliceosome
Current Biology, 1993The removal of introns from mRNA precursors (premRNA) is a complex process that takes place in the nucleus in a multi-component structure known as the spliceosome. The spliceosome is comparable in size and complexity to the ribosome and is mainly comprised of four RNA-protein complexes, the Ul, U2, U4/U6 and U5 small nuclear ribonucleoprotein particles
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Mechanisms of Spliceosomal Assembly
2014Pre-mRNA splicing is a key step for generating mature protein-coding mRNA. An RNA-protein complex known as the spliceosome carries out the chemistry of pre-mRNA splicing. However, several pre-spliceosomal intermediates are assembled on the pre-mRNA before the formation of the catalytically activated spliceosome.
Ni-Ting Chiou, Kristen W. Lynch
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Nature Chemical Biology, 2007
The U2 snRNP particle is an essential component of the eukaryotic pre-mRNA splicing apparatus, the spliceosome. Natural and semisynthetic inhibitors that bind the SF3b subunit of the U2 snRNP block splicing and prompt nuclear export of intron-bearing precursors, defining a new mode of action in anticancer drugs.
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The U2 snRNP particle is an essential component of the eukaryotic pre-mRNA splicing apparatus, the spliceosome. Natural and semisynthetic inhibitors that bind the SF3b subunit of the U2 snRNP block splicing and prompt nuclear export of intron-bearing precursors, defining a new mode of action in anticancer drugs.
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Spliceosome Assembly and Composition
2007Cells control alternative splicing by modulating assembly of the pre-mRNA splicing machinery at competing splice sites. Therefore, a working knowledge of spliceosome assembly is essential for understanding how alternative splice site choices are achieved.
Melissa J. Moore, Arianne J. Matlin
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Nature Structural & Molecular Biology, 2013
Two structural variants of the RNaseH-like domain of the highly conserved spliceosomal protein Prp8 are correlated with Prp8 mutants that stabilize either the first- or second-step active sites of the spliceosome.
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Two structural variants of the RNaseH-like domain of the highly conserved spliceosomal protein Prp8 are correlated with Prp8 mutants that stabilize either the first- or second-step active sites of the spliceosome.
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Radical probing of spliceosome assembly
Methods, 2017Here we describe the synthesis and use of a directed hydroxyl radical probe, tethered to a pre-mRNA substrate, to map the structure of this substrate during the spliceosome assembly process. These studies indicate an early organization and proximation of conserved pre-mRNA sequences during spliceosome assembly.
Andrew M. MacMillan+2 more
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The spliceosome: a ribozyme at heart?
bchm, 2007Abstract The spliceosome, the multi-megadalton molecular machine that performs splicing, consists of over 200 different proteins and five small nuclear RNAs (snRNAs). Extensive mechanistic and structural similarities to self-splicing group II introns, large ribozymes found in prokaryotes and lower eukaryotes that catalyze an identical ...
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Structure of the human spliceosome
Science, 2018Structural Biology Catalyzed by the spliceosome, precursor mRNA splicing proceeds in two steps: branching and exon ligation. Transition from the C (catalytic post-branching spliceosome) to the C* (catalytic pre-exon ligation spliceosome) complex is driven by the adenosine triphosphatase/helicase Prp16. Zhan et al.
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Structure and function of the spliceosome
Science, 2015Structural Biology 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.
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