Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleus (Q24304152)

peptidyl-arginine N-methylation

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Small nuclear ribonucleoprotein D3

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Small nuclear ribonucleoprotein B

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Protein arginine N-methyltransferase 5

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Small nuclear ribonucleoprotein D1

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author name string

Tina Branscombe Miranda

1

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Permanan Khusial

2

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Jeffry R Cook

3

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Jin-Hyung Lee

4

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Samuel I Gunderson

5

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Sidney Pestka

6

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Gary W Zieve

7

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Steven Clarke

Biochemical and Biophysical Research Communications

8

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language of work or name

English

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publication date

15 October 2004

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published in

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volume

323

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issue

2

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page(s)

382-7

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cites work

U2 RNA shares a structural domain with U1, U4, and U5 RNAs

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Thirteen anti-Sm monoclonal antibodies immunoprecipitate the three cytoplasmic snRNP core protein precursors in six distinct subsets

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Protein composition of mammalian spliceosomal snRNPs

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Cap trimethylation of U snRNA is cytoplasmic and dependent on U snRNP protein binding

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Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs

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Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln

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A biochemical function for the Sm complex.

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SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets

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Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.

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cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: evidence for a direct D1-D2 interaction

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The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity

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

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The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies

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PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins

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

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Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1

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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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Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation

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Arginine methylation facilitates the nuclear export of hnRNP proteins

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m3G cap hypermethylation of U1 small nuclear ribonucleoprotein (snRNP) in vitro: evidence that the U1 small nuclear RNA-(guanosine-N2)-methyltransferase is a non-snRNP cytoplasmic protein that requires a binding site on the Sm core domain

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The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins

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Cell biology of the snRNP particles

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