Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions. - Wikidata - awgldk - TriplyDB

Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions.

Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions.

http://www.wikidata.org/entity/Q30791977

about

Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications Molecular dissection of mRNA poly(A) tail length control in yeast RGG motif proteins: modulators of mRNA functional states Unphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.Yeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p.Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae.The shuttling protein Npl3 promotes translation termination accuracy in Saccharomyces cerevisiae.Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles.Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation.A conditional two-hybrid (C2H) system for the detection of protein-protein interactions that are mediated by post-translational modification.Asymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src.Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASF Enhanced methylarginine characterization by post-translational modification-specific targeted data acquisition and electron-transfer dissociation mass spectrometry.Identification of small-molecule enhancers of arginine methylation catalyzed by coactivator-associated arginine methyltransferase 1.Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo.Identification of a novel lipin homologue from the parasitic protozoan Trypanosoma brucei.Arginine methylation regulates mitochondrial gene expression in Trypanosoma brucei through multiple effector proteins.Arginine methylation of the RGG box does not appear to regulate ICP27 import during herpes simplex virus infection.Protein arginine methylation in Candida albicans: role in nuclear transport.Subcellular distribution of human RDM1 protein isoforms and their nucleolar accumulation in response to heat shock and proteotoxic stress Yeast cap binding complex impedes recruitment of cleavage factor IA to weak termination sites.Nuclear RNA surveillance: role of TRAMP in controlling exosome specificity.Autoregulation of Npl3, a yeast SR protein, requires a novel downstream region and serine phosphorylation Protein arginine methyltransferases: from unicellular eukaryotes to humans Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication.Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function.Methylation of yeast ribosomal protein S2 is elevated during stationary phase growth conditions.The methylproteome and the intracellular methylation network.Protein arginine methylation in Saccharomyces cerevisiae.Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.Arginine methylation of the nuclear poly(a) binding protein weakens the interaction with its nuclear import receptor, transportin.The Role of Protein Arginine Methylation in mRNP Dynamics Temporal and spatial regulation of mRNA export: Single particle RNA-imaging provides new tools and insights.Novel 3,5-bis(bromohydroxybenzylidene)piperidin-4-ones as coactivator-associated arginine methyltransferase 1 inhibitors: enzyme selectivity and cellular activity.Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively methylated and are substrates of the arginine methyltransferase Hmt1p.Yeast hnRNP-related proteins contribute to the maintenance of telomeres.Monosome formation during translation initiation requires the serine/arginine-rich protein Npl3.Protein arginine methylation facilitates cotranscriptional recruitment of pre-mRNA splicing factors.Site-specific and regiospecific installation of methylarginine analogues into recombinant histones and insights into effector protein binding Amphiphilic polyethylenimine polymers mediate efficient delivery of DNA and siRNA in mammalian cells.

P2860

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P2860

Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions.

http://www.wikidata.org/entity/Q30791977

description

2005 nî lūn-bûn

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2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի հուլիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Arginine methylation of yeast ...... anuclear protein interactions.

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Arginine methylation of yeast ...... anuclear protein interactions.

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type

label

Arginine methylation of yeast ...... anuclear protein interactions.

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Arginine methylation of yeast ...... anuclear protein interactions.

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prefLabel

Arginine methylation of yeast ...... anuclear protein interactions.

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Arginine methylation of yeast ...... anuclear protein interactions.

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P1433

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P1433

Journal of Biological Chemistry

P1476

Arginine methylation of yeast ...... anuclear protein interactions.

@en

P2093

Anne E McBride

http://www.w3.org/2001/XMLSchema#string

Elizabeth A Stemmler

http://www.w3.org/2001/XMLSchema#string

Jeffrey A Rubens

http://www.w3.org/2001/XMLSchema#string

Jeffrey T Cook

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Kate L Rutledge

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Kelly A McGrath

http://www.w3.org/2001/XMLSchema#string

P2860

TREX is a conserved complex coupling transcription with messenger RNA export

Histone deimination antagonizes arginine methylation

Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination

A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae.

A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins.

Nuclear export of hnRNP Hrp1p and nuclear export of hnRNP Npl3p are linked and influenced by the methylation state of Npl3p.

Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p.

A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export.

Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p

Arginine methylation facilitates the nuclear export of hnRNP proteins

P304

30888-30898

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scholarly article

P356

10.1074/JBC.M505831200

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P433

35

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P478

280

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P577

2005-07-05T00:00:00Z

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P698

15998636

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