File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Yeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p

TitleYeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p
Authors
Issue Date2010
PublisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/
Citation
Nucleic Acids Research, 2010, v. 38 n. 7, p. 2217-2228 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/124520
ISSN
2014 Impact Factor: 9.112
2014 SCImago Journal Rankings: 6.160
PubMed Central ID
ISI Accession Number ID
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.

References
Grants

 

DC FieldValueLanguage
dc.contributor.authorWong, CMen_HK
dc.contributor.authorTang, HMVen_HK
dc.contributor.authorKong, KYEen_HK
dc.contributor.authorWong, GWOen_HK
dc.contributor.authorQiu, Hen_HK
dc.contributor.authorJin, DYen_HK
dc.contributor.authorHinnebusch, AGen_HK
dc.date.accessioned2010-10-31T10:39:03Z-
dc.date.available2010-10-31T10:39:03Z-
dc.date.issued2010en_HK
dc.identifier.citationNucleic Acids Research, 2010, v. 38 n. 7, p. 2217-2228en_HK
dc.identifier.issn0305-1048en_HK
dc.identifier.urihttp://hdl.handle.net/10722/124520-
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.en_HK
dc.languageengen_HK
dc.publisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/en_HK
dc.relation.ispartofNucleic Acids Researchen_HK
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 Npl3pen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0305-1048&volume=38&issue=7&spage=2217&epage=2228&date=2010&atitle=Yeast+arginine+methyltransferase+Hmt1p+regulates+transcription+elongation+and+termination+by+methylating+Npl3pen_HK
dc.identifier.emailWong, CM:wispwong@hkucc.hku.hken_HK
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_HK
dc.identifier.authorityWong, CM=rp01489en_HK
dc.identifier.authorityJin, DY=rp00452en_HK
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1093/nar/gkp1133en_HK
dc.identifier.pmid20053728en_HK
dc.identifier.pmcidPMC2853106-
dc.identifier.scopuseid_2-s2.0-77952305539en_HK
dc.identifier.hkuros175811en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77952305539&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume38en_HK
dc.identifier.issue7en_HK
dc.identifier.spage2217en_HK
dc.identifier.epage2228en_HK
dc.identifier.eissn1362-4962-
dc.identifier.isiWOS:000276744600020-
dc.publisher.placeUnited Kingdomen_HK
dc.relation.projectCharacterization of fusion oncoprotein FUS-CREB3L2 found in soft tissue sarcoma-
dc.identifier.scopusauthoridWong, CM=18134632400en_HK
dc.identifier.scopusauthoridTang, HMV=35328375400en_HK
dc.identifier.scopusauthoridKong, KYE=36089940000en_HK
dc.identifier.scopusauthoridWong, GWO=25931696100en_HK
dc.identifier.scopusauthoridQiu, H=7201608807en_HK
dc.identifier.scopusauthoridJin, DY=7201973614en_HK
dc.identifier.scopusauthoridHinnebusch, AG=7005728566en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats