title: Escherichia coli transcription termination factor NusA: heat-induced oligomerization and chaperone activity.
abstract: Escherichia coli NusA, an essential component of the RNA polymerase elongation complex, is involved in transcriptional elongation, termination, anti-termination, cold shock and stress-induced mutagenesis. In this study, we demonstrated that NusA can self-assemble into oligomers under heat shock conditions and that this property is largely determined by the C-terminal domain. In parallel with the self-assembly process, NusA also acquires chaperone activity. Furthermore, NusA overexpression results in the enhanced heat shock resistance of host cells, which may be due to the chaperone activity of NusA. Our results suggest that E. coli NusA can act as a protector to prevent protein aggregation under heat stress conditions in vitro and in the NusA-overexpressing strain. We propose a new hypothesis that NusA could serve as a molecular chaperone in addition to its functions as a transcription factor. However, it remains to be further investigated whether NusA has the same function under normal physiological conditions.
authors.affiliation: State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Science, Beijing 100101, People's Republic of China.
authors.forename: Kun
authors.initials: K
authors.lastname: Li
authors.forename: Tianyi
authors.initials: T
authors.lastname: Jiang
authors.forename: Bo
authors.initials: B
authors.lastname: Yu
authors.forename: Limin
authors.initials: L
authors.lastname: Wang
authors.forename: Chao
authors.initials: C
authors.lastname: Gao
authors.forename: Cuiqing
authors.initials: C
authors.lastname: Ma
authors.forename: Ping
authors.initials: P
authors.lastname: Xu
authors.forename: Yanhe
authors.initials: Y
authors.lastname: Ma
mesh_terms: D019281:Dimerization; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006360:Heat-Shock Proteins / Q000737:chemistry*; D006358:Hot Temperature; D018832:Molecular Chaperones; D010445:Peptide Elongation Factors / Q000737:chemistry*; D011485:Protein Binding; D014157:Transcription Factors / Q000737:chemistry*; D061806:Transcription Termination, Genetic; D035602:Transcriptional Elongation Factors
chemical_list: D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D010445:Peptide Elongation Factors; D014157:Transcription Factors; D035602:Transcriptional Elongation Factors; C068727:nusA protein, E coli
references.citation: Cell. 2004 May 28;117(5):625-35
references.pmid: 15163410
references.citation: Biochemistry. 2003 Nov 25;42(46):13429-37
references.pmid: 14621988
references.citation: J Biol Chem. 1992 Jan 25;267(3):1449-54
references.pmid: 1370474
references.citation: J Biol Chem. 2004 Jul 30;279(31):32957-67
references.pmid: 15169774
references.citation: Nature. 1999 Nov 11;402(6758):147-54
references.pmid: 10647006
references.citation: New Phytol. 2011 Aug;191(3):692-705
references.pmid: 21564098
references.citation: Curr Biol. 2010 Jan 12;20(1):80-5
references.pmid: 20036541
references.citation: PLoS One. 2012;7(12):e47521
references.pmid: 23251328
references.citation: Nucleic Acids Res. 2009 Aug;37(14):4736-42
references.pmid: 19515940
references.citation: Appl Environ Microbiol. 2000 Dec;66(12):5306-11
references.pmid: 11097906
references.citation: BMB Rep. 2008 Feb 29;41(2):108-11
references.pmid: 18315945
references.citation: J Biol Chem. 2000 Jan 14;275(2):855-60
references.pmid: 10625618
references.citation: Biotechnol Bioeng. 1999 Nov 20;65(4):382-8
references.pmid: 10506413
references.citation: Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13762-7
references.pmid: 15365170
references.citation: Science. 2008 May 16;320(5878):935-8
references.pmid: 18487194
references.citation: Proc Natl Acad Sci U S A. 2006 Feb 21;103(8):2552-7
references.pmid: 16481626
references.citation: FEBS Lett. 2010 Jan 4;584(1):159-65
references.pmid: 19913538
references.citation: J Mol Biol. 1991 Jul 20;220(2):325-33
references.pmid: 1856862
references.citation: Protein Sci. 2005 Aug;14(8):2018-29
references.pmid: 15987884
references.citation: EMBO J. 2005 Oct 19;24(20):3576-87
references.pmid: 16193062
references.citation: Transcription. 2011 May;2(3):130-134
references.pmid: 21922055
references.citation: Appl Environ Microbiol. 2009 Sep;75(18):6008-12
references.pmid: 19633117
references.citation: J Bacteriol. 2011 Nov;193(22):6422-3
references.pmid: 22038975
references.citation: Proc Natl Acad Sci U S A. 1988 Apr;85(8):2494-8
references.pmid: 2965813
references.citation: Gene. 2003 Apr 10;308:115-28
references.pmid: 12711396
references.citation: EMBO J. 1999 Dec 15;18(24):6934-49
references.pmid: 10601016
references.citation: J Mol Biol. 2001 Dec 14;314(5):1087-95
references.pmid: 11743725
references.citation: Curr Genet. 2007 Jul;52(1):45-53
references.pmid: 17581753
references.citation: EMBO J. 1997 Jan 15;16(2):221-9
references.pmid: 9029143
references.citation: Gene. 2009 Jul 1;440(1-2):9-15
references.pmid: 19328840
references.citation: Science. 1999 Feb 5;283(5403):833-6
references.pmid: 9933164
references.citation: Biochemistry. 2006 Apr 11;45(14):4542-9
references.pmid: 16584189
references.citation: Proc Natl Acad Sci U S A. 1981 Feb;78(2):1115-8
references.pmid: 6453343
references.citation: J Biol Chem. 2010 Apr 9;285(15):11489-97
references.pmid: 20145254
references.citation: J Bacteriol. 1988 Feb;170(2):908-15
references.pmid: 2828334
references.citation: J Biol Chem. 1998 May 8;273(19):11478-82
references.pmid: 9565560
references.citation: Nature. 2000 Aug 31;406(6799):959-64
references.pmid: 10984043
references.citation: J Biol Chem. 2008 Jun 27;283(26):18385-92
references.pmid: 18430731
references.citation: Nat Struct Mol Biol. 2005 Oct;12(10):842-6
references.pmid: 16205709
references.citation: Mol Microbiol. 2001 Apr;40(2):397-413
references.pmid: 11309122
references.citation: Proc Natl Acad Sci U S A. 2010 Aug 31;107(35):15517-22
references.pmid: 20696893
references.citation: J Bacteriol. 2011 Sep;193(17):4563-4
references.pmid: 21705584
references.citation: Planta. 2003 Sep;217(5):813-9
references.pmid: 12743825
references.citation: Proc Natl Acad Sci U S A. 2009 Apr 7;106(14):5978-83
references.pmid: 19293385
references.citation: Proc Natl Acad Sci U S A. 2008 Aug 12;105(32):11329-34
references.pmid: 18678916
references.citation: Angew Chem Int Ed Engl. 2002 Apr 2;41(7):1098-113
references.pmid: 12491239
references.citation: Proc Natl Acad Sci U S A. 2002 Aug 20;99(17):11067-72
references.pmid: 12161562
references.citation: EMBO J. 1993 Nov;12(11):4137-44
references.pmid: 7900997
references.citation: Proc Natl Acad Sci U S A. 2009 Apr 7;106(14):5557-62
references.pmid: 19321422
references.citation: Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W321-6
references.pmid: 15215403
references.citation: Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7543-7
references.pmid: 8052617
references.citation: Protein Sci. 2003 Jun;12(6):1262-70
references.pmid: 12761397
references.citation: J Biol Chem. 1997 Dec 12;272(50):31636-40
references.pmid: 9395504
references.citation: J Mol Biol. 1991 Jul 20;220(2):307-24
references.pmid: 1856861
references.citation: J Mol Biol. 1987 Jun 20;195(4):809-18
references.pmid: 2821282