Structural Basis for Stabilization of the Hypervariable D3 Domain of Salmonella Flagellin upon Filament Formation

Journal of Molecular Biology

Volumn 403, Issue 4, 2010, Pages 607-615

  Muskotál, Adél ^a   Seregélyes, Csaba ^a   Sebestyén, Anett ^b   Vonderviszt, Ferenc ^a,b,c  

^a UNIVERSITY OF PANNONIA   (Hungary)

^b RESEARCH INSTITUTE FOR TECHNICAL PHYSICS AND MATERIALS SCIENCE   (Hungary)

^c INSTITUTE OF ENZYMOLOGY   (Hungary)

Author keywords

Filament stability; Flagellar filament; Flagellin; Hypervariable domain; Scanning calorimetry

Indexed keywords

FLAGELLIN; HYBRID PROTEIN; POLYMER; CROSS LINKING REAGENT; PRIMER DNA; RECOMBINANT PROTEIN;

ARTICLE; CROSS LINKING; DISULFIDE BOND; FLAGELLUM; GENE DELETION; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; SALMONELLA; THERMOSTABILITY; CHEMICAL STRUCTURE; CHEMISTRY; DIFFERENTIAL SCANNING CALORIMETRY; GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM; THERMODYNAMICS;

SALMONELLA;

BASE SEQUENCE; CALORIMETRY, DIFFERENTIAL SCANNING; CROSS-LINKING REAGENTS; DNA PRIMERS; FLAGELLIN; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SALMONELLA TYPHIMURIUM; SEQUENCE DELETION; THERMODYNAMICS;

EID: 77957895200     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.09.024     Document Type: Article

References (22)

1. Kanto S., Okino H., Aizawa S., Yamaguchi S. Amino acids responsible for flagellar shape are distributed in terminal regions of flagellin. J. Mol. Biol. 1991, 219:471-480.
2. Vonderviszt F., Kanto S., Aizawa S., Namba K. Terminal regions of flagellin are disordered in solution. J. Mol. Biol. 1989, 209:127-133.
3. Kostyukova A.S., Pyatibratov M.G., Filimonov V.V., Fedorov O.V. Flagellin parts acquiring a regular structure during polymerization are disposed on the molecule ends. FEBS Lett. 1988, 241:141-144.
4. Vonderviszt F., Uedaira H., Kidokoro S.I. Structural organization of flagellin. J. Mol. Biol. 1990, 214:97-104.
5. Yonekura K., Maki-Yonekura S., Namba K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 2003, 424:643-650.
6. Yamashita I., Hasegawa K., Suzuki H., Vonderviszt F., Mimori-Kiyosue Y., Namba K. Structure and switching of bacterial flagellar filaments studied by X-ray fiber diffraction. Nat. Struct. Biol. 1998, 5:125-132.
7. Samatey F.A., Imada K., Nagashima S., Vonderviszt F., Kumasaka T., Yamamoto M., Namba K. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature 2001, 410:331-337.
8. Beatson S.A., Minamino T., Pallen M.J. Variation in bacterial flagellins: from sequence to structure. Trends Microbiol. 2006, 14:151-155.
9. Honda S., Uedaira H., Vonderviszt F., Kidokoro S., Namba K. Folding energetics of a multidomain protein, flagellin. J. Mol. Biol. 1999, 293:719-732.
10. Sebestyén A, Muskotál A, Végh BM, Vonderviszt F. The hypervariable D3 domain of Salmonella flagellin is an autonomous folding unit. Protein Pept. Lett. 2008, 15:54-57.
11. Diószeghy Z., Závodszky P., Namba K., Vonderviszt F. Stabilization of flagellar filaments by HAP2 capping. FEBS Lett. 2004, 568:105-109.
12. Kuwajima G. Construction of a minimum-size functional flagellin of Escherichia coli. J. Bacteriol. 1988, 170:3305-3309.
13. Malapaka R.R., Adebayo L.O., Tripp B.C. A deletion variant study of the functional role of the Salmonella flagellin hypervariable domain region in motility. J. Mol. Biol. 2007, 365:1102-1116.
14. Yoshioka K., Aizawa S., Yamaguchi S. Flagellar filament structure and cell motility of Salmonella typhimurium mutants lacking part of the outer domain of flagellin. J. Bacteriol. 1995, 177:1090-1093.
15. Mimori-Kiyosue Y., Yamashita I., Fujiyoshi Y., Yamaguchi S., Namba K. Role of the outermost subdomain of Salmonella flagellin in the filament structure revealed by electron cryomicroscopy. J. Mol. Biol. 1997, 270:222-237.
16. Iino T. Assembly of Salmonella flagellin in vitro and in vivo. J. Supramol. Struct. 1974, 2:372-384.
17. Eswar N., Marti-Renom M.A., Webb B., Madhusudhan M.S., Eramian D., Shen M., et al. Comparative protein structure modeling with MODELLER. Current Protocols in Bioinformatics 2006, suppl. 15, chapt. 5:5.6.1-5.6.30. John Wiley & Sons, Inc.
18. Dombkowski A.A. Disulfide by design: a computational method for the rational design of disulfide bonds in proteins. Bioinformatics 2003, 19:1852-1853.
19. Stocker B.A, Newton S.M. Immune responses to epitopes inserted in Salmonella flagellin. Int. Rev. Immunol. 1994, 11:167-178.
20. Westerlund-Wikstrom B. Peptide display on bacterial flagella: principles and applications. Int. J. Med. Microbiol. 2000, 290:223-230.
21. Cattozo E.M., Stocker B.A., Radaelli A., De Giuli Morghen C, Tognon M. Expression and immunogenicity of V3 loop epitopes of HIV-1, isolates SC and WMJ2, inserted in Salmonella flagellin. J. Biotechnol. 1997, 56:191-203.
22. Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A. Protein identification and analysis tools on the ExPASy server. The Proteomics Protocols Handbook 2005, 571-607. Humana Press Inc., Totowa, NJ. J.M. Walker (Ed.).