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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
2005-8-29
pubmed:abstractText
Arginine methylation can affect both nucleocytoplasmic transport and protein-protein interactions of RNA-binding proteins. These effects are seen in cells that lack the yeast hnRNP methyltransferase (HMT1), raising the question of whether effects on specific proteins are direct or indirect. The presence of multiple arginines in individual methylated proteins also raises the question of whether overall methylation or methylation of a subset of arginines affects protein function. We have used the yeast mRNA-binding protein Npl3 to address these questions in vivo. Matrix-assisted laser desorption/ionization Fourier transform mass spectrometry was used to identify 17 methylated arginines in Npl3 purified from yeast: whereas 10 Arg-Gly-Gly (RGG) tripeptides were exclusively dimethylated, variable levels of methylation were found for 5 RGG and 2 RG motif arginines. We constructed a set of Npl3 proteins in which subsets of the RGG arginines were mutated to lysine. Expression of these mutant proteins as the sole form of Npl3 specifically affected growth of a strain that requires Hmt1. Although decreased growth generally correlated with increased numbers of Arg-to-Lys mutations, lysine substitutions in the N terminus of the RGG domain showed more severe effects. Npl3 with all 15 RGG arginines mutated to lysine exited the nucleus independent of Hmt1, indicating a direct effect of methylation on Npl3 transport. These mutations also resulted in a decreased, methylation-independent interaction of Npl3 with transcription elongation factor Tho2 and inhibited Npl3 self-association. These results support a model in which arginine methylation facilitates Npl3 export directly by weakening contacts with nuclear proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30888-98
pubmed:dateRevised
2009-6-10
pubmed:meshHeading
pubmed-meshheading:15998636-Active Transport, Cell Nucleus, pubmed-meshheading:15998636-Amino Acid Sequence, pubmed-meshheading:15998636-Arginine, pubmed-meshheading:15998636-Humans, pubmed-meshheading:15998636-Lysine, pubmed-meshheading:15998636-Methylation, pubmed-meshheading:15998636-Molecular Sequence Data, pubmed-meshheading:15998636-Mutagenesis, Site-Directed, pubmed-meshheading:15998636-Nuclear Proteins, pubmed-meshheading:15998636-Peptides, pubmed-meshheading:15998636-Protein Interaction Mapping, pubmed-meshheading:15998636-RNA-Binding Proteins, pubmed-meshheading:15998636-Saccharomyces cerevisiae Proteins, pubmed-meshheading:15998636-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:15998636-Spectroscopy, Fourier Transform Infrared, pubmed-meshheading:15998636-Transcription Factors
pubmed:year
2005
pubmed:articleTitle
Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions.
pubmed:affiliation
Department of Biology, Bowdoin College, Brunswick, Maine 04011, USA. amcbride@bowdoin.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't