Structure and function of an RNase H domain at the heart of the spliceosome - Test2 - elhamkhani - TriplyDB

Structure and function of an RNase H domain at the heart of the spliceosome

Structure and function of an RNase H domain at the heart of the spliceosome

http://www.wikidata.org/entity/Q27652459

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Cwc2 and its human homologue RBM22 promote an active conformation of the spliceosome catalytic centre Pre-mRNA Splicing in Plants: In Vivo Functions of RNA-Binding Proteins Implicated in the Splicing Process Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2 Mechanism for Aar2p function as a U5 snRNP assembly factor Crystal structure of Prp8 reveals active site cavity of the spliceosome Structural basis for dual roles of Aar2p in U5 snRNP assembly Crystal structure of Cwc2 reveals a novel architecture of a multipartite RNA-binding protein A conformational switch in PRP8 mediates metal ion coordination that promotes pre-mRNA exon ligation Structural Basis of Brr2-Prp8 Interactions and Implications for U5 snRNP Biogenesis and the Spliceosome Active Site Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8 Molecular architecture of the human U4/U6.U5 tri-snRNP The DExD/H-box ATPase Prp2p destabilizes and proofreads the catalytic RNA core of the spliceosome.Comprehensive in vivo RNA-binding site analyses reveal a role of Prp8 in spliceosomal assembly.Rapid screening of yeast mutants with reporters identifies new splicing phenotypes.CEF1/CDC5 alleles modulate transitions between catalytic conformations of the spliceosome.The RNase H-like superfamily: new members, comparative structural analysis and evolutionary classification.Spliceosome Structure and Function Prp8, the pivotal protein of the spliceosomal catalytic center, evolved from a retroelement-encoded reverse transcriptase The reverse transcriptase-RNase H: from viruses to antiviral defense.Mechanisms and Regulation of Alternative Pre-mRNA Splicing Retroviral integrase superfamily: the structural perspective.Functional roles of protein splicing factors.Spliceosome activation: U4 is the path, stem I is the goal, and Prp8 is the keeper. Let's cheer for the ATPase Brr2!Conformational heterogeneity of the protein-free human spliceosomal U2-U6 snRNA complex ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the C terminus of Prp8.The spliceosome as ribozyme hypothesis takes a second step.Model systems: how chemical biologists study RNA.Splicing of mRNA precursors: the role of RNAs and proteins in catalysis.Structural insights into RNA splicing.Nucleases: diversity of structure, function and mechanism.The spliceosomal proteome: at the heart of the largest cellular ribonucleoprotein machine.Structural analyses of the pre-mRNA splicing machinery Structural studies of the spliceosome: zooming into the heart of the machine.Novel regulatory principles of the spliceosomal Brr2 RNA helicase and links to retinal disease in humans.A snRNP's ordered path to maturity.Functional consequences of splicing of the antisense transcript COOLAIR on FLC transcription.Functions and regulation of the Brr2 RNA helicase during splicing.Real time monitoring of junction ribonuclease activity of RNase H using chimeric molecular beacons.Crystallization and biochemical characterization of the human spliceosomal Aar2-Prp8(RNaseH) complex.Emerging views about the molecular structure of the spliceosomal catalytic center.

P2860

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P2860

Structure and function of an RNase H domain at the heart of the spliceosome

http://www.wikidata.org/entity/Q27652459

description

2008 nî lūn-bûn

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2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Structure and function of an RNase H domain at the heart of the spliceosome

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Structure and function of an RNase H domain at the heart of the spliceosome

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Structure and function of an RNase H domain at the heart of the spliceosome

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type

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Structure and function of an RNase H domain at the heart of the spliceosome

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Structure and function of an RNase H domain at the heart of the spliceosome

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Structure and function of an RNase H domain at the heart of the spliceosome

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prefLabel

Structure and function of an RNase H domain at the heart of the spliceosome

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Structure and function of an RNase H domain at the heart of the spliceosome

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Structure and function of an RNase H domain at the heart of the spliceosome

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The EMBO Journal

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Structure and function of an RNase H domain at the heart of the spliceosome

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P2093

Alexey Rozov

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Patrizia Fabrizio

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Vladimir Pena

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P2860

The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein

CASK Functions as a Mg2+-independent neurexin kinase

The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro

Prp8 protein: at the heart of the spliceosome

Prp16p, Slu7p, and Prp8p interact with the 3' splice site in two distinct stages during the second catalytic step of pre-mRNA splicing

The canonical GU dinucleotide at the 5' splice site is recognized by p220 of the U5 snRNP within the spliceosome

The C-terminal region of hPrp8 interacts with the conserved GU dinucleotide at the 5' splice site

Characterization of U6 snRNA-protein interactions.

A general two-metal-ion mechanism for catalytic RNA

Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases

P304

2929-40

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scholarly article

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10.1038/EMBOJ.2008.209

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21

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27

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Reinhard Georg Lührmann

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2008-11-05T00:00:00Z

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23307653

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18843295

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2580788

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