Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. (Q33888183)

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3 November 2019

title

Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions (English)

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3 November 2019

4

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3 November 2019

author name string

A E McBride

1

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3 November 2019

V H Weiss

2

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3 November 2019

H K Kim

3

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3 November 2019

P A Silver

5

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3 November 2019

language of work or name

English

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publication date

1 February 2000

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Journal of Biological Chemistry

3 November 2019

number of pages

9

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inferred from page(s)

published in

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3 November 2019

volume

275

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3 November 2019

issue

5

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3 November 2019

page(s)

3128-3136

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The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase

3 November 2019

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

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A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor

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S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase

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Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors

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Identification of N(G)-methylarginine residues in human heterogeneous RNP protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe is a preferred recognition motif

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Arginine methylation facilitates the nuclear export of hnRNP proteins

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Protein methylation in animal cells. I. Purification and properties of S-adenosyl-L-methionine:protein (arginine) N-methyltransferase from Krebs II ascites cells

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Methylases of myelin basic protein and histone in rat brain

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In vivo and in vitro arginine methylation of RNA-binding proteins

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Purification and characterization of S-adenosylmethionine-protein-arginine N-methyltransferase from rat liver

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Specific Enzymic Methylation of an Arginine in the Experimental Allergic Encephalomyelitis Protein from Human Myelin

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Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes

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Universal catalytic domain structure of AdoMet-dependent methyltransferases.

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Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)

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The essential yeast RNA binding protein Np13p is methylated

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

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NOP3 is an essential yeast protein which is required for pre-rRNA processing

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A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast

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Hrp1, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3′-end formation in yeast

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Arginine methylation and binding of Hrp1p to the efficiency element for mRNA 3'-end formation.

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RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases.

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A yeast cap binding protein complex (yCBC) acts at an early step in pre-mRNA splicing.

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A nuclear cap-binding complex facilitates association of U1 snRNP with the cap-proximal 5' splice site.

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The Role of the Cap Structure in RNA Processing and Nuclear Export

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A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine

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