Structural insights into chaperone addiction of toxin-antitoxin systems.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
15 02 2019
15 02 2019
Historique:
received:
21
05
2018
accepted:
10
01
2019
entrez:
17
2
2019
pubmed:
17
2
2019
medline:
9
4
2019
Statut:
epublish
Résumé
SecB chaperones assist protein export by binding both unfolded proteins and the SecA motor. Certain SecB homologs can also control toxin-antitoxin (TA) systems known to modulate bacterial growth in response to stress. In such TA-chaperone (TAC) systems, SecB assists the folding and prevents degradation of the antitoxin, thus facilitating toxin inhibition. Chaperone dependency is conferred by a C-terminal extension in the antitoxin known as chaperone addiction (ChAD) sequence, which makes the antitoxin aggregation-prone and prevents toxin inhibition. Using TAC of Mycobacterium tuberculosis, we present the structure of a SecB-like chaperone bound to its ChAD peptide. We find differences in the binding interfaces when compared to SecB-SecA or SecB-preprotein complexes, and show that the antitoxin can reach a functional form while bound to the chaperone. This work reveals how chaperones can use discrete surface binding regions to accommodate different clients or partners and thereby expand their substrate repertoire and functions.
Identifiants
pubmed: 30770830
doi: 10.1038/s41467-019-08747-4
pii: 10.1038/s41467-019-08747-4
pmc: PMC6377645
doi:
Substances chimiques
Bacterial Proteins
0
Molecular Chaperones
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
782Commentaires et corrections
Type : ErratumIn
Références
Bioinformatics. 2000 Jun;16(6):566-7
pubmed: 10980157
PLoS One. 2008 Jan 02;3(1):e1403
pubmed: 18167562
Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55
pubmed: 15299926
Science. 2014 Jan 10;343(6167):204-8
pubmed: 24408438
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501
pubmed: 20383002
Biophys J. 2008 Apr 15;94(8):3258-65
pubmed: 18199676
FEMS Microbiol Rev. 2016 Sep;40(5):592-609
pubmed: 27476076
J Biol Chem. 1999 Nov 26;274(48):34219-25
pubmed: 10567394
Front Microbiol. 2014 Dec 05;5:666
pubmed: 25538690
J Biol Chem. 1995 Oct 27;270(43):25920-7
pubmed: 7592780
mBio. 2018 Jun 12;9(3):
pubmed: 29895634
Proc Natl Acad Sci U S A. 2004 May 18;101(20):7583-8
pubmed: 15128935
J Struct Biol. 2003 Dec;144(3):313-9
pubmed: 14643199
J Bacteriol. 2010 Sep;192(17):4348-56
pubmed: 20585061
Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3
pubmed: 15299374
Nucleic Acids Res. 2010 Jul;38(Web Server issue):W545-9
pubmed: 20457744
Nucleic Acids Res. 2017 May 5;45(8):4972-4983
pubmed: 28334932
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42
pubmed: 21460441
J Biol Chem. 2014 Jan 10;289(2):1060-70
pubmed: 24257752
Nucleic Acids Res. 2012 Oct;40(19):9927-40
pubmed: 22844099
J Appl Crystallogr. 2017 Jun 26;50(Pt 4):1212-1225
pubmed: 28808438
mBio. 2017 Dec 12;8(6):
pubmed: 29233898
Mol Microbiol. 2002 Feb;43(3):717-31
pubmed: 11929527
Cell Mol Life Sci. 2002 Oct;59(10):1617-23
pubmed: 12475171
Sci Rep. 2017 Jan 27;7:41341
pubmed: 28128357
Annu Rev Microbiol. 2010;64:357-72
pubmed: 20528688
Mol Cell. 2016 Jul 7;63(1):86-96
pubmed: 27264868
Nat Struct Biol. 2000 Dec;7(12):1172-7
pubmed: 11101901
FEMS Microbiol Rev. 2015 Jul;39(4):522-40
pubmed: 25796610
Pathog Dis. 2014 Aug;71(3):326-35
pubmed: 24719230
mBio. 2011 Jun 14;2(3):e00100-11
pubmed: 21673191
EMBO Rep. 2004 Feb;5(2):195-200
pubmed: 14726952
Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3101-6
pubmed: 17360615
Proc Natl Acad Sci U S A. 2011 May 17;108(20):8438-43
pubmed: 21536872
Proc Natl Acad Sci U S A. 2017 Nov 21;114(47):12584-12589
pubmed: 29114057
Acta Crystallogr F Struct Biol Commun. 2016 Jun;72(Pt 6):457-61
pubmed: 27303898
J Mol Biol. 2007 Jan 5;365(1):1-9
pubmed: 17055530
Cell Stress Chaperones. 2013 Mar;18(2):129-35
pubmed: 23264229
Chem Rev. 2007 Aug;107(8):3544-67
pubmed: 17649985
Anal Chem. 2015 Apr 21;87(8):4370-6
pubmed: 25799115
PLoS Genet. 2009 Dec;5(12):e1000767
pubmed: 20011113
J Chem Theory Comput. 2013 Jul 9;9(7):3084-95
pubmed: 26583988
PLoS Pathog. 2012;8(10):e1002954
pubmed: 23055930
J Mol Biol. 2007 Sep 21;372(3):774-97
pubmed: 17681537
Annu Rev Genet. 2011;45:61-79
pubmed: 22060041
Microbiology. 2002 Oct;148(Pt 10):3129-3138
pubmed: 12368446
Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1002-11
pubmed: 16929101
Cell. 2011 Jan 7;144(1):143-56
pubmed: 21185072
Trends Biochem Sci. 1995 Feb;20(2):65-9
pubmed: 7701564
Nat Commun. 2016 Nov 09;7:13339
pubmed: 27827369
Toxins (Basel). 2014 Mar 06;6(3):1002-20
pubmed: 24662523
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):293-302
pubmed: 21460447
Toxins (Basel). 2014 Jan 10;6(1):304-24
pubmed: 24434905
Nature. 2013 Apr 25;496(7446):477-81
pubmed: 23619693
Protein Sci. 2004 Apr;13(4):1124-33
pubmed: 15010547
J Bacteriol. 1989 Feb;171(2):813-8
pubmed: 2644237
Nat Struct Biol. 2003 Nov;10(11):942-7
pubmed: 14517549
Genetics. 1993 Apr;133(4):763-73
pubmed: 8462840
Microbiology. 2009 Jan;155(Pt 1):186-197
pubmed: 19118359
Gene. 1995 Sep 22;163(1):41-6
pubmed: 7557476
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
pubmed: 19461840
J Mol Biol. 2006 Oct 13;363(1):63-74
pubmed: 16962134
Nature. 2016 Sep 8;537(7619):202-206
pubmed: 27501151
Nucleic Acids Res. 2014 Jul;42(Web Server issue):W320-4
pubmed: 24753421
J Bacteriol. 1995 Jul;177(14):4121-30
pubmed: 7608087