A bacterial-like mechanism for transcription termination by the Sen1p helicase in budding yeast.
Odil Porrua, Domenico Libri
Author Information
Odil Porrua: Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique, Gif sur Yvette, France. porrua-f@cgm.cnrs-gif.fr
中文译文
English
Transcription termination is essential to generate functional RNAs and to prevent disruptive polymerase collisions resulting from concurrent transcription. The yeast Sen1p helicase is involved in termination of most noncoding RNAs transcribed by RNA polymerase II (RNAPII). However, the mechanism of termination and the role of this protein have remained enigmatic. Here we address the mechanism of Sen1p-dependent termination by using a highly purified in vitro system. We show that Sen1p is the key enzyme of the termination reaction and reveal features of the termination mechanism. Like the bacterial termination factor Rho, Sen1p recognizes the nascent RNA and hydrolyzes ATP to dissociate the elongation complex. Sen1p-dependent termination is highly specific and, notably, does not require the C-terminal domain of RNAPII. We also show that termination is inhibited by RNA-DNA hybrids. Our results elucidate the role of Sen1p in controlling pervasive transcription.
Nature. 2006 Dec 14;444(7121):953-6
[PMID: 17128255 ]
Nature. 2001 Sep 20;413(6853):327-31
[PMID: 11565036 ]
J Biol Chem. 2001 Dec 14;276(50):47150-3
[PMID: 11591727 ]
J Biol Chem. 2000 Mar 3;275(9):6530-6
[PMID: 10692458 ]
Mol Cell Biol. 1992 May;12(5):2154-64
[PMID: 1569945 ]
Genetics. 2010 Jan;184(1):107-18
[PMID: 19884310 ]
Mol Cell. 2006 Dec 8;24(5):735-746
[PMID: 17157256 ]
Eukaryot Cell. 2012 Apr;11(4):417-29
[PMID: 22286094 ]
EMBO J. 2011 May 4;30(9):1790-803
[PMID: 21460797 ]
Mol Cell Biol. 2006 Apr;26(7):2688-96
[PMID: 16537912 ]
Protein Expr Purif. 2005 May;41(1):207-34
[PMID: 15915565 ]
Curr Opin Struct Biol. 2010 Jun;20(3):313-24
[PMID: 20456941 ]
Genes Dev. 2005 Jul 1;19(13):1572-80
[PMID: 15998810 ]
Nat Struct Mol Biol. 2010 Oct;17(10):1195-201
[PMID: 20818393 ]
Orphanet J Rare Dis. 2006 Nov 17;1:47
[PMID: 17112370 ]
Trends Biochem Sci. 2011 Jan;36(1):19-29
[PMID: 20813532 ]
Mol Cell Biol. 2007 Apr;27(8):2821-9
[PMID: 17296737 ]
Genes Dev. 2008 Apr 15;22(8):1082-92
[PMID: 18413718 ]
Trends Biochem Sci. 2007 Apr;32(4):165-71
[PMID: 17349792 ]
Nat Struct Mol Biol. 2008 Dec;15(12):1263-71
[PMID: 19011635 ]
PLoS Genet. 2011 Oct;7(10):e1002329
[PMID: 22028667 ]
Nature. 1993 Jul 29;364(6436):401-6
[PMID: 8332211 ]
Adv Protein Chem. 2004;67:1-42
[PMID: 14969722 ]
Genet Res Int. 2011;2011:653494
[PMID: 22567365 ]
J Mol Biol. 2010 Feb 5;395(5):966-82
[PMID: 20026069 ]
Mol Cell. 2009 Jun 26;34(6):710-21
[PMID: 19560423 ]
Science. 2012 Jun 29;336(6089):1723-5
[PMID: 22745433 ]
Genes Dev. 2012 Sep 1;26(17):1891-6
[PMID: 22892239 ]
Cell. 1982 Jul;29(3):877-86
[PMID: 7151173 ]
Mol Cell. 2006 Sep 15;23(6):853-64
[PMID: 16973437 ]
Mol Cell. 2011 Jun 24;42(6):794-805
[PMID: 21700224 ]
Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4900-5
[PMID: 9560200 ]
Nature. 2003 Oct 16;425(6959):737-41
[PMID: 14562106 ]
Biochim Biophys Acta. 2006 Nov-Dec;1762(11-12):986-1000
[PMID: 16765570 ]
Methods Enzymol. 2012;511:255-74
[PMID: 22713324 ]
Nature. 2004 Nov 25;432(7016):522-5
[PMID: 15565158 ]
Cell. 2012 Sep 14;150(6):1147-57
[PMID: 22980978 ]
Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6075-8
[PMID: 9177171 ]
J Mol Biol. 2011 Oct 7;412(5):793-813
[PMID: 21439297 ]
Mol Cell. 2006 Sep 15;23(6):841-51
[PMID: 16973436 ]
J Cell Biol. 2007 Jun 18;177(6):969-79
[PMID: 17562789 ]
Biochemistry. 1999 Nov 2;38(44):14697-710
[PMID: 10545196 ]
Proc Natl Acad Sci U S A. 1987 Dec;84(23):8306-10
[PMID: 3479794 ]
Nat Struct Mol Biol. 2007 Sep;14(9):796-806
[PMID: 17676063 ]
Nat Struct Mol Biol. 2008 Aug;15(8):786-94
[PMID: 18660821 ]
Mol Cell. 2011 Mar 18;41(6):693-703
[PMID: 21419344 ]
Mol Cell. 2009 Oct 23;36(2):255-66
[PMID: 19854134 ]
Mol Cell. 2001 May;7(5):1013-23
[PMID: 11389848 ]
EMBO J. 2012 Oct 3;31(19):3935-48
[PMID: 23032188 ]
Nature. 2004 Nov 25;432(7016):517-22
[PMID: 15565157 ]
Mol Cell. 2013 Jan 10;49(1):55-66
[PMID: 23177741 ]
Nature. 2010 Jan 14;463(7278):245-9
[PMID: 20075920 ]
Mol Cell. 2011 Jan 7;41(1):21-32
[PMID: 21211720 ]
Nat Struct Mol Biol. 2008 Aug;15(8):795-804
[PMID: 18660819 ]
Nat Rev Genet. 2009 Dec;10(12):833-44
[PMID: 19920851 ]
Cell. 2005 Jun 3;121(5):725-37
[PMID: 15935759 ]
Mol Cell. 2006 Dec 8;24(5):723-734
[PMID: 17157255 ]
Nat Biotechnol. 1999 Oct;17(10):1030-2
[PMID: 10504710 ]
Adenosine Triphosphate
Base Sequence
DNA Helicases
DNA-Binding Proteins
Models, Genetic
Molecular Sequence Data
Multiprotein Complexes
Nuclear Proteins
Protein Structure, Tertiary
RNA Helicases
RNA Polymerase II
RNA Precursors
RNA, Fungal
RNA, Small Nucleolar
RNA-Binding Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Species Specificity
Transcription Factors
Transcription Termination, Genetic
DNA-Binding Proteins
Multiprotein Complexes
NAB3 protein, S cerevisiae
NRD1 protein, S cerevisiae
Nuclear Proteins
REB1 protein, S cerevisiae
RNA Precursors
RNA, Fungal
RNA, Small Nucleolar
RNA-Binding Proteins
Saccharomyces cerevisiae Proteins
Transcription Factors
Adenosine Triphosphate
RNA Polymerase II
SEN1 protein, S cerevisiae
DNA Helicases
RNA Helicases