Article: Yeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p
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- Publisher Website: 10.1093/nar/gkp1133
- Scopus: eid_2-s2.0-77952305539
- PMID: 20053728
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| Title | Yeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Authors | Wong, CM1 Tang, HMV1 Kong, KYE1 Wong, GWO1 Qiu, H2 Jin, DY1 Hinnebusch, AG2 | ||||||||
| Issue Date | 2010 | ||||||||
| Publisher | Oxford 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?] DOI: http://dx.doi.org/10.1093/nar/gkp1133 | ||||||||
| Abstract | The 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. | ||||||||
| Description | The eleventh Meeting on Transcriptional Regulation in Eukaryotes, Cold Spring Harbor Laboratory, 25-29 August 2009 | ||||||||
| ISSN | 0305-1048 2011 Impact Factor: 8.026 2011 SCImago Journal Rankings: 1.542 | ||||||||
| DOI | http://dx.doi.org/10.1093/nar/gkp1133 | ||||||||
| ISI Accession Number ID | WOS:000276744600020
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. | ||||||||
| PubMed Central ID | PMC2853106 | ||||||||
| References | References in Scopus | ||||||||
| Grants | Characterization of fusion oncoprotein FUS-CREB3L2 found in soft tissue sarcoma |
| dc.contributor.author | Wong, CM | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| dc.contributor.author | Tang, HMV | ||||||||
| dc.contributor.author | Kong, KYE | ||||||||
| dc.contributor.author | Wong, GWO | ||||||||
| dc.contributor.author | Qiu, H | ||||||||
| dc.contributor.author | Jin, DY | ||||||||
| dc.contributor.author | Hinnebusch, AG | ||||||||
| dc.date.accessioned | 2010-10-31T10:39:03Z | ||||||||
| dc.date.available | 2010-10-31T10:39:03Z | ||||||||
| dc.date.issued | 2010 | ||||||||
| dc.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'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.grant | Characterization of fusion oncoprotein FUS-CREB3L2 found in soft tissue sarcoma | ||||||||
| dc.description.grantcode | 82365 | ||||||||
| dc.description.nature | published_or_final_version | ||||||||
| dc.description | The eleventh Meeting on Transcriptional Regulation in Eukaryotes, Cold Spring Harbor Laboratory, 25-29 August 2009 | ||||||||
| dc.identifier.citation | Nucleic Acids Research, 2010, v. 38 n. 7, p. 2217-2228 [How to Cite?] DOI: http://dx.doi.org/10.1093/nar/gkp1133 | ||||||||
| dc.identifier.doi | http://dx.doi.org/10.1093/nar/gkp1133 | ||||||||
| dc.identifier.epage | 2228 | ||||||||
| dc.identifier.hkuros | 175811 | ||||||||
| dc.identifier.isi | WOS:000276744600020
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.issn | 0305-1048 2011 Impact Factor: 8.026 2011 SCImago Journal Rankings: 1.542 | ||||||||
| dc.identifier.issue | 7 | ||||||||
| dc.identifier.openurl | | ||||||||
| dc.identifier.pmcid | PMC2853106 | ||||||||
| dc.identifier.pmid | 20053728 | ||||||||
| dc.identifier.scopus | eid_2-s2.0-77952305539 | ||||||||
| dc.identifier.spage | 2217 | ||||||||
| dc.identifier.uri | http://hdl.handle.net/10722/124520 | ||||||||
| dc.identifier.volume | 38 | ||||||||
| dc.language | eng | ||||||||
| dc.publisher | Oxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/ | ||||||||
| dc.publisher.place | United Kingdom | ||||||||
| dc.relation.ispartof | Nucleic Acids Research | ||||||||
| dc.relation.references | References in Scopus | ||||||||
| dc.subject.mesh | Gene Expression Regulation | ||||||||
| dc.subject.mesh | Nuclear Proteins - chemistry - metabolism | ||||||||
| dc.subject.mesh | Protein-Arginine N-Methyltransferases - genetics - metabolism | ||||||||
| dc.subject.mesh | RNA-Binding Proteins - chemistry - metabolism | ||||||||
| dc.subject.mesh | Repressor Proteins - genetics - metabolism | ||||||||
| dc.title | Yeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p | ||||||||
| dc.type | Article |
Author Affiliations
- The University of Hong Kong
- National Institute of Child Health and Human Development