Bacterial conjugation
Bifunctional enzyme
NMR spectroscopy
Plasmid R1
TraI
Journal
Biomolecular NMR assignments
ISSN: 1874-270X
Titre abrégé: Biomol NMR Assign
Pays: Netherlands
ID NLM: 101472371
Informations de publication
Date de publication:
04 2019
04 2019
Historique:
received:
25
09
2018
accepted:
04
12
2018
pubmed:
9
1
2019
medline:
20
8
2019
entrez:
9
1
2019
Statut:
ppublish
Résumé
Transfer of genetic material is the main mechanism underlying the spread of antibiotic resistance and virulence factors within the bacterial community. Conjugation is one such process by which the genetic material is shared from one bacterium to another. The DNA substrate is processed and prepared for transfer by a multi-protein complex called the relaxosome .The relaxosome of plasmid R1 possesses the most crucial enzyme TraI which, both nicks and unwinds the dsDNA substrate. TraI comprises 1765 residues and multiple functional domains, including those catalyzing the DNA trans-esterase (relaxase) on the dsDNA designated for a conjugative transfer and DNA helicase activities. Structural and functional studies have been reported for most of the TraI except the C-terminal domain spanning from residue 1630 to 1765. This region is the least understood part of TraI and is thought to be highly disordered and flexible. This region, being intrinsically disordered, is hypothesized to be serving as an interacting platform for other proteins involved in this DNA transfer initiation mechanism. In this work, we report the
Identifiants
pubmed: 30617945
doi: 10.1007/s12104-018-9863-y
pii: 10.1007/s12104-018-9863-y
pmc: PMC6439144
doi:
Substances chimiques
Bacterial Proteins
0
Carbon Isotopes
0
Nitrogen Isotopes
0
Nitrogen-15
0
Protons
0
Carbon-13
FDJ0A8596D
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Pagination
121-125Références
Bogomolovas J, Simon B, Sattler M, Stier G (2009) Screening of fusion partners for high yield expression and purification of bioactive viscotoxins. Protein Expr Purif 64(1):16–23
doi: 10.1016/j.pep.2008.10.003
Cheng Y, McNamara DE, Miley MJ, Nash RP, Redinbo MR (2011) Functional characterization of the multidomain F Plasmid trai relaxase-helicase. J Biol Chem Apr 8(14):12670–12682
doi: 10.1074/jbc.M110.207563
Christie PJ, Gomez Valero L, Buchrieser C (2017) Biological diversity and evolution of type IV secretion systems. Curr Top Microbiol Immunol 413:1–30
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277–293
doi: 10.1007/BF00197809
Guogas LM1, Kennedy SA, Lee JH, Redinbo MR (2009) A novel fold in the TraI relaxase-helicase c-terminal domain is essential for conjugative DNA transfer. J Mol Biol 20(2):554–568
doi: 10.1016/j.jmb.2008.12.057
Haft RJ1, Palacios G, Nguyen T, Mally M, Gachelet EG, Zechner EL, Traxler B (2006) General mutagenesis of F plasmid TraI reveals its role in conjugative regulation. J Bacteriol 188(17):6346–6353
doi: 10.1128/JB.00462-06
Ilangovan A, Connery S, Waksman G (2015) Structural biology of the Gram-negative bacterial conjugation systems. Trends Microbiol 23(5):301–310
doi: 10.1016/j.tim.2015.02.012
Ilangovan A, Kay CWM, Roier S, El Mkami H, Salvadori E, Zechner EL, Zanetti G, Waksman G (2017) Cryo-EM structure of a relaxase reveals the molecular basis of DNA unwinding during bacterial conjugation. Cell 4(4):708–721
doi: 10.1016/j.cell.2017.04.010
John, Cavanagh et al (2006) Protein NMR spectroscopy, 2nd edn. Academic Press, Cambridge
Lang S, Gruber K, Mihajlovic S, Arnold R, Gruber CJ, Steinlechner S, Jehl MA, Rattei T, Fröhlich KU, Zechner EL (2010) Molecular recognition determinants for type IV secretion of diverse families of conjugative relaxases. Mol Microbiol 78(6):1539–1555
doi: 10.1111/j.1365-2958.2010.07423.x
Lang S, Kirchberger PC, Gruber CJ, Redzej A, Raffl S, Zellnig G, Zangger K, Zechner EL (2011) An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation. Mol Microbiol 82(5):1071–1085
doi: 10.1111/j.1365-2958.2011.07872.x
Lawley TD, Klimke WA, Gubbins MJ, Frost LS (2003) F factor conjugation is a true type IV secretion system. FEMS Microbial Lett 15(1):1–15
doi: 10.1016/S0378-1097(03)00430-0
M9 minimal medium (standard) (2010) Cold spring harbor protocols. http://cshprotocols.cshlp.org/content/2010/8/pdb.rec12295.short . Accessed 20 Sept 2018
Matson SW, Ragonese H (2005) The F-plasmid TraI protein contains three functional domains required for conjugative DNA strand transfer. J Bacteriol 187(2):697–706
doi: 10.1128/JB.187.2.697-706.2005
Ragonese H, Haisch D, Villareal E, Choi JH, Matson SW (2007) The F plasmid-encoded TraM protein stimulates relaxosome-mediated cleavage at oriT through an interaction with TraI. Mol Microbiol 63(4):1173–1184
doi: 10.1111/j.1365-2958.2006.05576.x
Shen Y, Bax A (2013) Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks. J Biomol NMR 56(3):227–241
doi: 10.1007/s10858-013-9741-y
Vranken WF et al (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 1(4):687–696
doi: 10.1002/prot.20449
Wong JJ, Lu J, Glover JN (2012) Relaxosome function and conjugation regulation in F-like plasmids—a structural biology perspective. Mol Microbiol 85(4):602–617
doi: 10.1111/j.1365-2958.2012.08131.x