title: Full repression of RNA polymerase III transcription requires interaction between two domains of its negative regulator Maf1.
abstract: Maf1, first identified in yeast Saccharomyces cerevisiae, is a general negative regulator of RNA polymerase III (Pol III). Transcription regulation by Maf1 is important under stress conditions and during the switch between fermentation and respiration. Maf1 is composed of two domains conserved during evolution. We report here that these two domains of human Maf1 are resistant to mild proteolysis and interact together as shown by pull-down and size-exclusion chromatography and that the comparable domains of yeast Maf1 interact in a two-hybrid assay. Additionally, in yeast, a mutation in the N-terminal domain is compensated by mutations in the C-terminal domain. Integrity of both domains and their direct interaction are necessary for Maf1 dephosphorylation and subsequent inhibition of Pol III transcription on a nonfermentable carbon source. These data relate Pol III transcription inhibition to Maf1 structural changes.
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland.
authors.forename: Anna
authors.initials: A
authors.lastname: Gajda
authors.forename: Joanna
authors.initials: J
authors.lastname: Towpik
authors.forename: Ulrich
authors.initials: U
authors.lastname: Steuerwald
authors.forename: Christoph W
authors.initials: CW
authors.lastname: Müller
authors.forename: Olivier
authors.initials: O
authors.lastname: Lefebvre
authors.forename: Magdalena
authors.initials: M
authors.lastname: Boguta
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D015152:Blotting, Northern; D002478:Cells, Cultured; D002850:Chromatography, Gel; D005786:Gene Expression Regulation; D006801:Humans; D015151:Immunoblotting; D008969:Molecular Sequence Data; D009154:Mutation; D010766:Phosphorylation; D011485:Protein Binding; D012320:RNA Polymerase III / Q000378:metabolism*; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic / Q000235:genetics*; D020798:Two-Hybrid System Techniques
chemical_list: C104954:MAF1 protein, S cerevisiae; C520535:MAF1 protein, human; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D012320:RNA Polymerase III
references.citation: Cold Spring Harb Symp Quant Biol. 2001;66:567-74
references.pmid: 12762058
references.citation: Mol Cell Biol. 2001 Aug;21(15):5031-40
references.pmid: 11438659
references.citation: Nucleic Acids Res. 2005 Jul 1;33(Web Server issue):W36-8
references.pmid: 15980489
references.citation: Cell. 2008 Apr 4;133(1):78-89
references.pmid: 18394991
references.citation: Mol Cell. 2007 May 11;26(3):367-79
references.pmid: 17499043
references.citation: PLoS One. 2006 Dec 27;1:e134
references.pmid: 17205138
references.citation: J Mol Biol. 2008 May 2;378(3):481-91
references.pmid: 18377933
references.citation: Genes Dev. 2002 Oct 15;16(20):2593-620
references.pmid: 12381659
references.citation: Prog Nucleic Acid Res Mol Biol. 2004;77:323-53
references.pmid: 15196897
references.citation: Gene. 1997 Feb 7;185(2):291-6
references.pmid: 9055829
references.citation: Genetics. 1989 May;122(1):19-27
references.pmid: 2659436
references.citation: Genes Dev. 2009 Aug 15;23(16):1929-43
references.pmid: 19684113
references.citation: EMBO J. 2003 Sep 15;22(18):4738-47
references.pmid: 12970186
references.citation: Trends Genet. 2008 Dec;24(12):622-9
references.pmid: 18980784
references.citation: J Biol Chem. 2009 May 8;284(19):12604-8
references.pmid: 19299514
references.citation: Mol Cell Biol. 1998 Jun;18(6):3191-200
references.pmid: 9584160
references.citation: J Biol Chem. 2008 Jun 20;283(25):17168-74
references.pmid: 18445601
references.citation: J Mol Biol. 1999 Sep 17;292(2):195-202
references.pmid: 10493868
references.citation: J Biol Chem. 2005 Feb 25;280(8):6455-62
references.pmid: 15590667
references.citation: Mol Cell. 2006 Jun 9;22(5):623-32
references.pmid: 16762835
references.citation: Mol Cell Biol. 2004 May;24(10):4118-27
references.pmid: 15121834
references.citation: Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14695-700
references.pmid: 14634212
references.citation: Mol Cell. 2006 Jun 9;22(5):633-44
references.pmid: 16762836
references.citation: J Mol Biol. 2001 Jun 29;310(1):1-26
references.pmid: 11419933
references.citation: J Mol Biol. 1999 Dec 17;294(5):1351-62
references.pmid: 10600390
references.citation: Int J Biol Sci. 2007 May 01;3(5):292-302
references.pmid: 17505538
references.citation: Nucleic Acids Res. 1990 May 25;18(10):3091-2
references.pmid: 2190191
references.citation: Methods Enzymol. 2002;350:3-41
references.pmid: 12073320
references.citation: Cell Cycle. 2008 Nov 1;7(21):3327-9
references.pmid: 18971635
references.citation: Eukaryot Cell. 2009 Sep;8(9):1429-38
references.pmid: 19581440
references.citation: J Biol Chem. 2008 Jul 11;283(28):19184-91
references.pmid: 18456653
references.citation: Cell Mol Life Sci. 1997 Aug;53(8):621-45
references.pmid: 9351466
references.citation: Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15044-9
references.pmid: 17005718
references.citation: Trends Biochem Sci. 1999 Nov;24(11):437-40
references.pmid: 10542411
references.citation: Cell. 1993 Nov 19;75(4):805-16
references.pmid: 8242751
references.citation: Nat Rev Cancer. 2008 Dec;8(12):911-4
references.pmid: 18987635
references.citation: Mol Cell Biol. 2007 Nov;27(21):7693-702
references.pmid: 17785443
references.citation: Mol Cell. 2002 Dec;10(6):1489-94
references.pmid: 12504022
references.citation: Yeast. 1992 Feb;8(2):79-82
references.pmid: 1561838
references.citation: J Biol Chem. 1993 Oct 5;268(28):20721-4
references.pmid: 8407894