Mutagenesis and chemical cross-linking suggest that Wzz dimer stability and oligomerization affect lipopolysaccharide O-antigen modal chain length control

Journal of Bacteriology

Volumn 192, Issue 13, 2010, Pages 3385-3393

  Papadopoulos, Magdalene ^a   Morona, Renato ^a  

^a UNIVERSITY OF ADELAIDE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; DIMER; DODECYL SULFATE SODIUM; FORMALDEHYDE; LIPOPOLYSACCHARIDE; O ANTIGEN; PROTEIN WZZ; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CROSS LINKING; DNA SEQUENCE; GENE INSERTION; GENE MAPPING; HEATING; IN VIVO STUDY; MOLECULAR STABILITY; MOLECULAR WEIGHT; MUTAGENESIS; MUTANT; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN STABILITY; SHIGELLA FLEXNERI; WILD TYPE;

BACTERIAL PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; MUTAGENESIS; O ANTIGENS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; SHIGELLA FLEXNERI;

SHIGELLA FLEXNERI;

EID: 77954361463     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01134-09     Document Type: Article

References (26)

1. Bastin, D. A., L. K. Romana, and P. R. Reeves. 1991. Molecular cloning and expression in Escherichia coli K-12 of the rfb gene cluster determining the O antigen of an E. coli O111 strain. Mol. Microbiol. 5:2223-2231.
2. Becker, A., H. Kuster, K. Niehaus, and A. Puhler. 1995. Extension of the Rhizobium meliloti succinoglycan biosynthesis gene cluster: identification of the exsA gene encoding an ABC transporter protein, and the exsB gene which probably codes for a regulator of succinoglycan biosynthesis. Mol. Gen. Genet. 249:487-497.
3. Becker, A., and A. Puhler. 1998. Specific amino acid substitutions in the proline-rich motif of the Rhizobium meliloti ExoP protein result in enhanced production of low-molecular-weight succinoglycan at the expense of high-molecular-weight succinoglycan. J. Bacteriol. 180:395-399.
4. Daniels, C., and R. Morona. 1999. Analysis of Shigella flexneri Wzz (Rol) function by mutagenesis and cross-linking: Wzz is able to oligomerize. Mol. Microbiol. 34:181-194.
5. Daniels, C., C. Vindurampulle, and R. Morona. 1998. Overexpression and topology of the Shigella flexneri O-antigen polymerase (Rfc/Wzy). Mol. Microbiol. 28:1211-1222.
6. Franco, A. V., D. Liu, and P. R. Reeves. 1998. The Wzz (Cld) protein in Escherichia coli: amino acid sequence variation determines O-antigen chain length specificity. J. Bacteriol. 180:2670-2675.
7. Guo, H., K. Lokko, Y. Zhang, W. Yi, Z. Wu, and P. G. Wang. 2006. Overexpression and characterization of Wzz of Escherichia coli O86:H2. Protein Expr. Purif 48:49-55.
8. Hong, M., and S. M. Payne. 1997. Effect of mutations in Shigella flexneri chromosomal and plasmid-encoded lipopolysaccharide genes on invasion and serum resistance. Mol. Microbiol. 24:779-791.
9. Larue, K., M. S. Kimber, R. Ford, and C. Whitfield. 2009. Biochemical and structural analysis of bacterial O-antigen chain length regulator proteins reveals a conserved quaternary structure. J. Biol. Chem. 284:7395-7403.
10. Lugtenberg, B., J. Meijers, R. Peters, P. van der Hoek, and L. van Alphen. 1975. Electrophoretic resolution of the "major outer membrane protein" of Escherichia coli K12 into four bands. FEBS Lett. 58:254-258.
11. Marolda, C. L., L. D. Tatar, C. Alaimo, M. Aebi, and M. A. Valvano. 2006. Interplay of the Wzx translocase and the corresponding polymerase and chain length regulator proteins in the translocation and periplasmic assembly of lipopolysaccharide O antigen. J. Bacteriol. 188:5124-5135.
12. Morona, R., L. Purins, A. Tocilj, A. Matte, and M. Cygler. 2009. Sequence-structure relationships in polysaccharide co-polymerase (PCP) proteins. Trends Biochem. Sci. 34:78-84.
13. Morona, R., L. Van Den Bosch, and C. Daniels. 2000. Evaluation of Wzz/ MPA1/MPA2 proteins based on the presence of coiled-coil regions. Microbiology 146:1-4. (Pubitemid 30066300)
14. Morona, R., L. Van Den Bosch, and P. A. Manning. 1995. Molecular, genetic, and topological characterization of O-antigen chain length regulation in Shigella flexneri. J. Bacteriol. 177:1059-1068.
15. Murray, G. L., S. R. Attridge, and R. Morona. 2003. Regulation of Salmonella typhimurium lipopolysaccharide O antigen chain length is required for virulence; identification of FepE as a second Wzz. Mol. Microbiol. 47:1395-1406.
16. Prossnitz, E., K. Nikaido, S. J. Ulbrich, and G. F. Ames. 1988. Formaldehyde and photoactivatable cross-linking of the periplasmic binding protein to a membrane component of the histidine transport system of Salmonella typhimurium. J. Biol. Chem. 263:17917-17920.
17. Purins, L., L. Van Den Bosch, V. Richardson, and R. Morona. 2008. Coiledcoil regions play a role in the function of the Shigella flexneri O-antigen chain length regulator WzzpHS2. Microbiology 154:1104-1116.
18. Raetz, C. R., and C. Whitfield. 2002. Lipopolysaccharide endotoxins. Annu. Rev. Biochem. 71:635-700.
19. Simmons, D. A. 1993. Genetic and biosynthetic aspects of Shigella flexneri O-specific lipopolysaccharides. Biochem. Soc. Trans. 21:58S.
20. Tang, K. H., H. Guo, W. Yi, M. D. Tsai, and P. G. Wang. 2007. Investigation of the conformational states of Wzz and the Wzz O-antigen complex under near-physiological conditions. Biochemistry 46:11744-11752.
21. Tocilj, A., C. Munger, A. Proteau, R. Morona, L. Purins, E. Ajamian, J. Wagner, M. Papadopoulos, L. Van Den Bosch, J. L. Rubinstein, J. Fethiere, A. Matte, and M. Cygler. 2008. Bacterial polysaccharide co-polymerases share a common framework for control of polymer length. Nat. Struct. Mol. Biol. 15:130-138.
22. Tsai, C. M., and C. E. Frasch. 1982. A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels. Anal. Biochem. 119:115-119.
23. Van Den Bosch, L., P. A. Manning, and R. Morona. 1997. Regulation of O-antigen chain length is required for Shigella flexneri virulence. Mol. Microbiol. 23:765-775.
24. Van Den Bosch, L., and R. Morona. 2003. The actin-based motility defect of a Shigella flexneri rmlD rough LPS mutant is not due to loss of IcsA polarity. Microb. Pathog. 35:11-18.
25. West, N. P., P. Sansonetti, J. Mounier, R. M. Exley, C. Parsot, S. Guadagnini, M. C. Prevost, A. Prochnicka-Chalufour, M. Delepierre, M. Tanguy, and C. M. Tang. 2005. Optimization of virulence functions through glucosylation of Shigella LPS. Science 307:1313-1317.
26. Whitfield, C., and J. H. Naismith. 2008. Periplasmic export machines for outer membrane assembly. Curr. Opin. Struct. Biol. 18:466-474.