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Article: Yeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p
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TitleYeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p
 
AuthorsWong, CM1
Tang, HMV1
Kong, KYE1
Wong, GWO1
Qiu, H2
Jin, DY1
Hinnebusch, AG2
 
Issue Date2010
 
PublisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/
 
CitationNucleic Acids Research, 2010, v. 38 n. 7, p. 2217-2228 [How to Cite?]
DOI: http://dx.doi.org/10.1093/nar/gkp1133
 
AbstractThe heterogeneous nuclear ribonucleoprotein Npl3p of budding yeast is a substrate of arginine methyltransferase Hmt1p, but the role of Hmt1p in regulating Npl3p's functions in transcription antitermination and elongation were unknown. We found that mutants lacking Hmt1p methyltransferase activity exhibit reduced recruitment of Npl3p, but elevated recruitment of a component of mRNA cleavage/termination factor CFI, to the activated GAL10-GAL7 locus. Consistent with this, hmt1 mutants displayed increased termination at the defective gal10-δ56 terminator. Remarkably, hmt1δ cells also exhibit diminished recruitment of elongation factor Tho2p and a reduced rate of transcription elongation in vivo. Importantly, the defects in Npl3p and Tho2p recruitment, antitermination and elongation in hmt1δ cells all were mitigated by substitutions in Npl3p RGG repeats that functionally mimic arginine methylation by Hmt1p. Thus, Hmt1p promotes elongation and suppresses termination at cryptic terminators by methylating RGG repeats in Npl3p. As Hmt1p stimulates dissociation of Tho2p from an Npl3p-mRNP complex, it could act to recycle these elongation and antitermination factors back to sites of ongoing transcription. © The Author(s) 2010. Published by Oxford University Press.
 
DescriptionThe eleventh Meeting on Transcriptional Regulation in Eukaryotes, Cold Spring Harbor Laboratory, 25-29 August 2009
 
ISSN0305-1048
2012 Impact Factor: 8.278
2012 SCImago Journal Rankings: 5.125
 
DOIhttp://dx.doi.org/10.1093/nar/gkp1133
 
PubMed Central IDPMC2853106
 
ISI Accession Number IDWOS:000276744600020
Funding AgencyGrant Number
University Research Committee of the University of Hong Kong
Hong Kong Research Grants CouncilHKU 7486/06M
NIH
Funding Information:

The University Research Committee of the University of Hong Kong; Hong Kong Research Grants Council (project HKU 7486/06M); Intramural Research Program of the NIH.

 
ReferencesReferences in Scopus
 
GrantsCharacterization of fusion oncoprotein FUS-CREB3L2 found in soft tissue sarcoma
 
DC FieldValue
dc.contributor.authorWong, CM
 
dc.contributor.authorTang, HMV
 
dc.contributor.authorKong, KYE
 
dc.contributor.authorWong, GWO
 
dc.contributor.authorQiu, H
 
dc.contributor.authorJin, DY
 
dc.contributor.authorHinnebusch, AG
 
dc.date.accessioned2010-10-31T10:39:03Z
 
dc.date.available2010-10-31T10:39:03Z
 
dc.date.issued2010
 
dc.description.abstractThe heterogeneous nuclear ribonucleoprotein Npl3p of budding yeast is a substrate of arginine methyltransferase Hmt1p, but the role of Hmt1p in regulating Npl3p's functions in transcription antitermination and elongation were unknown. We found that mutants lacking Hmt1p methyltransferase activity exhibit reduced recruitment of Npl3p, but elevated recruitment of a component of mRNA cleavage/termination factor CFI, to the activated GAL10-GAL7 locus. Consistent with this, hmt1 mutants displayed increased termination at the defective gal10-δ56 terminator. Remarkably, hmt1δ cells also exhibit diminished recruitment of elongation factor Tho2p and a reduced rate of transcription elongation in vivo. Importantly, the defects in Npl3p and Tho2p recruitment, antitermination and elongation in hmt1δ cells all were mitigated by substitutions in Npl3p RGG repeats that functionally mimic arginine methylation by Hmt1p. Thus, Hmt1p promotes elongation and suppresses termination at cryptic terminators by methylating RGG repeats in Npl3p. As Hmt1p stimulates dissociation of Tho2p from an Npl3p-mRNP complex, it could act to recycle these elongation and antitermination factors back to sites of ongoing transcription. © The Author(s) 2010. Published by Oxford University Press.
 
dc.description.naturepublished_or_final_version
 
dc.descriptionThe eleventh Meeting on Transcriptional Regulation in Eukaryotes, Cold Spring Harbor Laboratory, 25-29 August 2009
 
dc.identifier.citationNucleic Acids Research, 2010, v. 38 n. 7, p. 2217-2228 [How to Cite?]
DOI: http://dx.doi.org/10.1093/nar/gkp1133
 
dc.identifier.doihttp://dx.doi.org/10.1093/nar/gkp1133
 
dc.identifier.eissn1362-4962
 
dc.identifier.epage2228
 
dc.identifier.hkuros175811
 
dc.identifier.isiWOS:000276744600020
Funding AgencyGrant Number
University Research Committee of the University of Hong Kong
Hong Kong Research Grants CouncilHKU 7486/06M
NIH
Funding Information:

The University Research Committee of the University of Hong Kong; Hong Kong Research Grants Council (project HKU 7486/06M); Intramural Research Program of the NIH.

 
dc.identifier.issn0305-1048
2012 Impact Factor: 8.278
2012 SCImago Journal Rankings: 5.125
 
dc.identifier.issue7
 
dc.identifier.openurl
 
dc.identifier.pmcidPMC2853106
 
dc.identifier.pmid20053728
 
dc.identifier.scopuseid_2-s2.0-77952305539
 
dc.identifier.spage2217
 
dc.identifier.urihttp://hdl.handle.net/10722/124520
 
dc.identifier.volume38
 
dc.languageeng
 
dc.publisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofNucleic Acids Research
 
dc.relation.projectCharacterization of fusion oncoprotein FUS-CREB3L2 found in soft tissue sarcoma
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshGene Expression Regulation
 
dc.subject.meshNuclear Proteins - chemistry - metabolism
 
dc.subject.meshProtein-Arginine N-Methyltransferases - genetics - metabolism
 
dc.subject.meshRNA-Binding Proteins - chemistry - metabolism
 
dc.subject.meshRepressor Proteins - genetics - metabolism
 
dc.titleYeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p
 
dc.typeArticle
 
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<description.abstract>The heterogeneous nuclear ribonucleoprotein Npl3p of budding yeast is a substrate of arginine methyltransferase Hmt1p, but the role of Hmt1p in regulating Npl3p&apos;s functions in transcription antitermination and elongation were unknown. We found that mutants lacking Hmt1p methyltransferase activity exhibit reduced recruitment of Npl3p, but elevated recruitment of a component of mRNA cleavage/termination factor CFI, to the activated GAL10-GAL7 locus. Consistent with this, hmt1 mutants displayed increased termination at the defective gal10-&#948;56 terminator. Remarkably, hmt1&#948; cells also exhibit diminished recruitment of elongation factor Tho2p and a reduced rate of transcription elongation in vivo. Importantly, the defects in Npl3p and Tho2p recruitment, antitermination and elongation in hmt1&#948; cells all were mitigated by substitutions in Npl3p RGG repeats that functionally mimic arginine methylation by Hmt1p. Thus, Hmt1p promotes elongation and suppresses termination at cryptic terminators by methylating RGG repeats in Npl3p. As Hmt1p stimulates dissociation of Tho2p from an Npl3p-mRNP complex, it could act to recycle these elongation and antitermination factors back to sites of ongoing transcription. &#169; The Author(s) 2010. Published by Oxford University Press.</description.abstract>
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Author Affiliations
  1. The University of Hong Kong
  2. National Institute of Child Health and Human Development