FtsQ interaction mutants: A way to identify new antibacterial targets

New Biotechnology

Volumn 27, Issue 6, 2010, Pages 870-881

  Grenga, L ^a   Guglielmi, G ^a   Melino, S ^a   Ghelardini, P ^b   Paolozzi, L ^a  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

^b CNR   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBACTERIAL DRUGS; BIOLOGICAL ACTIVITIES; BIOLOGICAL SIGNIFICANCE; CELL DIVISIONS; CO-IMMUNOPRECIPITATION EXPERIMENTS; RANDOM MUTAGENESIS; TWO-HYBRID ASSAYS;

CELL PROLIFERATION; ESCHERICHIA COLI; MACHINE DESIGN; MACHINERY;

PROTEINS;

ANTIINFECTIVE AGENT; CELL CYCLE PROTEIN; CELL CYCLE PROTEIN FTSL; CELL CYCLE PROTEIN FTSQ; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; BIOLOGICAL ACTIVITY; ESCHERICHIA COLI; MUTAGENESIS; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE;

ANTI-BACTERIAL AGENTS; BACTERIAL INFECTIONS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENETIC COMPLEMENTATION TEST; HUMANS; MEMBRANE PROTEINS; POINT MUTATION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 78649338546     PISSN: 18716784     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbt.2010.05.002     Document Type: Article

References (33)

1. Kapoor S., Panda D. Targeting FtsZ for antibacterial therapy: a promising avenue. Science 2009, 321:1644-1645.
2. Lock R.L., Harry E.J. Cell division inhibitors: new insights for future antibiotics. Nat. Rev. Drug Discov. 2008, 7:324-338.
3. Vollmer W. The prokaryotic cytoskeleton: a putative target for inhibitors and antibiotics?. Appl. Microbiol. Biotechnol. 2006, 73:37-47.
4. Goehring N.W., Beckwith J. Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr. Biol. 2005, 15:R514-R526.
5. Vicente M., Rico A.I. The order of the ring: assembly of Escherichia coli cell division components. Mol. Microbiol. 2006, 61:5-8.
6. de Boer P., et al. The essential bacterial cell-division protein FtsZ is a Gtpase. Nature 1992, 359:254-256.
7. Löwe J., Amos L.A. Crystal structure of the bacterial cell-division protein FtsZ. Nature 1998, 391:203-206.
8. Lu C.L., et al. Straight and curved conformations of FtsZ are regulated by GTP hydrolysis. J. Bacteriol. 2000, 182:164-170.
9. Erickson H.P., et al. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:519-523.
10. Löwe J., Amos L.A. Tubulin-like protofilaments in Ca2+-induced FtsZ sheets. EMBO J. 1999, 18:2364-2371.
11. Mukherjee A., Lutkenhaus J. Guanine nucleotide-dependent assembly of FtsZ into filaments. J. Bacteriol. 1994, 176:2754-2758.
12. RayChaudhuri D., Park J.T. Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein. Nature 1992, 359:251-254.
13. Yu X.C., Margolin W. Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J. 1997, 16:5455-5463.
14. Aarsman M.E., et al. Maturation of the Escherichia coli divisome occurs in two steps. Mol. Microbiol. 2005, 55:1631-1645.
15. Chen J.C., Beckwith J. FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. Mol. Microbiol. 2001, 42:395-413.
16. Rico, A.I. et al. Role of Escherichia coli FtsN protein in the assembly and stability of the cell division ring. Mol. Microbiol. (in press).
17. Carson M.J., et al. The FtsQ protein of Escherichia coli: membrane topology, abundance, and cell division phenotypes due to overproduction and insertion mutations. J. Bacteriol. 1991, 173:2187-2195.
18. Guzman L.M., et al. Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli. J. Bacteriol. 1997, 179:5094-5103.
19. Sánchez-Pulido L., et al. POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. Trends Biochem. Sci. 2003, 28:523-526.
20. Robson S.A., King G.F. Domain architecture and structure of the bacterial cell division protein DivIB. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:6700-6705.
21. D'Ulisse V., et al. Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins. Microbiology 2007, 153:124-138.
22. Karimova G., et al. Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J. Bacteriol. 2005, 187:2233-2243.
23. van den Ent F., et al. Structural and mutational analysis of the cell division protein FtsQ. Mol. Microbiol. 2008, 68:110-123.
24. Wadsworth K.D., et al. The divisomal protein DivIB contains multiple epitopes that mediate its recruitment to incipient division sites. Mol. Microbiol. 2008, 67:1143-1165.
25. Miller J.H. Experiments in Molecular Genetics 1972, Cold Spring Harbor Laboratory.
26. Di Lallo G., et al. Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation. Microbiology 2003, 149:3353-3359.
27. Chen J.C., et al. Septal localization of FtsQ, an essential cell division protein in Escherichia coli. J. Bacteriol. 1999, 181:521-530.
28. Barbati S., et al. Prokaryotic division interactome: set up of an assay for protein-protein interaction mutant selection. Res. Microbiol. 2010, 161:118-126.
29. Lutz R., Bujard H. Independent and tight regulation of transcriptional units in Escherichia coli via the LacR/O, the TetR/O and AraC/I1-I2 regulatory elements. Nucleic Acid Res. 1997, 25:1203-1210.
30. Sambrook J., et al. Molecular Cloning: A Laboratory Manual 1989, Cold Spring Harbor Laboratory.
31. Fadda D., et al. Streptococcus pneumoniae DivIVA: localization and interactions in a MinCD-free context. J. Bacteriol. 2007, 189:1288-1298.
32. Maggi S., et al. Division protein interaction web: identification of a phylogenetically conserved common interactome between Streptococcus pneumoniae and Escherichia coli. Microbiology 2008, 154:3042-3052.
33. Buddelmeijer N., et al. Localization of cell division protein FtsQ by immunofluorescence microscopy in dividing and nondividing cells of Escherichia coli. J. Bacteriol. 1998, 180:6107-6116.