Cloning and characterization of three hypothetical secretion chaperone proteins from Xanthomonas axonopodis pv. citri

Protein Expression and Purification

Volumn 53, Issue 2, 2007, Pages 363-369

  Tasic, Ljubica ^a   Borin, Paula F L ^a   Khater, Letícia ^a,b   Ramos, Carlos H I ^b  

^a UNIVERSITY OF CAMPINAS   (Brazil)

^b LABORATÓRIO NACIONAL DE LUZ SÍNCROTRON   (Brazil)

Author keywords

Hypothetical secretion chaperones; Spectroscopic characterization; Xanthomonas axonopodis pv. citri

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; CHEMISTRY; CIRCULAR DICHROISM; CITRUS FRUIT; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; ISOLATION AND PURIFICATION; MICROBIOLOGY; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PATHOGENICITY; PLANT DISEASE; PROTEIN SECONDARY STRUCTURE; SPECTROFLUOROMETRY; VIRULENCE; XANTHOMONAS AXONOPODIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CIRCULAR DICHROISM; CITRUS; CLONING, MOLECULAR; ESCHERICHIA COLI; GENE EXPRESSION; GENES, BACTERIAL; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PLANT DISEASES; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; VIRULENCE; XANTHOMONAS AXONOPODIS;

CITRUS; ESCHERICHIA COLI; EUKARYOTA; XANTHOMONAS; XANTHOMONAS AXONOPODIS PV. CITRI;

EID: 33947400553     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.01.011     Document Type: Article

References (33)

1. da Silva A., Ferro J., Reinach F., Farah C., Furlan L., Quaggio R., Monteiro-Vitorello C., Van Sluys M., Almeida N., Alves L., do Amaral A., Bertolini M., Camargo L., Camarote G., Cannavan F., Cardozo J., Chambergo F., Ciapina L., Cicarelli R., Coutinho L., Cursino-Santos J., El-Dorry H., Faria J., Ferreira A., Ferreira R., Ferro M., Formighieri E., Franco M., Greggio C., Gruber A., Katsuyama A., Kishi L., Leite R., Lemos E., Lemos M., Locali E., Machado M., Madeira A., Martinez-Rossi N., Martins E., Meidanis J., Menck C., Miyaki C., Moon D., Moreira L., Novo M., Okura V., Oliveira M., Oliveira V., Pereira H., Rossi A., Sena J., Silva C., de Souza R., Spinola A., Takita M., Tamura R., Teixeira E., Tezza R., Trinidade dos Santos M., Truffi D., Tsai S., White F., Setúbal J., and Kitajima J. Comparison of the genomes of two Xanthomonas pathogens with differing host specificity. Nature 417 (2002) 459-463
2. Alegria M., Souza D., Andrade M., Docena C., Khater L., Ramos C., da Silva A., and Farah C. Identification of new protein-protein interactions involving the products of the chormosome- and plasmid-encoded type IV secretion loci of the phytopathogen Xanthomonas axonopodis pv. citri. J. Bacteriol. 187 (2005) 2315-2325
3. L. Khater, T. Santos, M. Alegria, C. Docena, A. da Silva, C. Ramos, In silico identification of potential chaperone genes that belong to type III and type IV secretion systems in Xanthomonas axonopodis pv. citri, Genet. Mol. Biol. 28 (2005) 321-327.
4. Alegria M., Docena C., Khater L., Ramos C., da Silva A., and Farah C. New protein-protein identified for the regulatory and structural components and substrates of the type III secretion system of the phytopathogen Xanthomonas axonopodis pathovar citri. J. Bacteriol. 186 (2004) 6186-6197
5. Cordes F., Daniell S., Kenjale R., Saurya S., Picking W., Picking W., Booy F., Lea S., and Blocker A. Helical packing of needles from functionally altered Shigella type III sectretion systems. J. Mol. Biol. 354 (2005) 206-211
6. Minamino T., and Macnab R. Components of the Salmonella flagellar export apparatus and classification of export substrates. J. Bactreiol. 181 (1999) 4207-4215
7. Brunings A., and Gabriel D. Xanthomonas citri: breaking the surface. Mol. Plant Pathol. 4 (2003) 141-157
8. Page A.-L., Sansonetti P., and Parsot C. Spa15 of Shigella flexneri, a third type of chaperone in the type III secretion pathway. Mol. Microbiol. 43 (2002) 1533-1542
9. Gálan J., and Collmer A. Type III secretion machines: bacterial devices for protein delivery into host cells. Science 284 (1999) 1322-1328
10. Stebbins C., and Gálan J. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414 (2001) 77-81
11. Pallen M., Francis M., and Fütterer K. Tetratricopeptide-like repeats in type-III secretion chaperones and regulators. FEMS Microbiol. Lett. 223 (2003) 53-60
12. Page A.-L., and Parsot C. Chaperones of type III secretion pathway: Jacks of all trades. Mol. Microbiol. 46 (2002) 1-11
13. Buttner D., and Bonas U. Getting across-bacterial type III effector proteins on their way to the plant cell. EMBO J. 21 (2002) 5313-5322
14. Lloyd S., Forsberg A., Wolf-Watz H., and Francis M. Targeting exported substrates to the Yersinia TTSS: different functions for different signals?. Trends Microbiol. 9 (2001) 367-371
15. MacNab R. How bacteria assemble flagella. Annu. Rev. Microbiol. 57 (2003) 77-100
16. Parsot C., Hamiaux C., and Page A.-L. The various and varying roles of specific chaperones in type III secretion systems. Curr. Opin. Microbiol. 6 (2003) 7-14
17. Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6 (1967) 1948-1954
18. Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
19. CDNN 2.1: Circular Dichroism Deconvolution, Neutral Networks (1999).
20. Deléage G., and Geourjon C. An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum. Comput. Appl. Biosci. 9 (1993) 197-199
21. Chen Y., Yang J., and Chau K. Determination of the helix and β-form of proteins in aqueous solution by circular dichroism. Biochemistry 13 (1974) 3350-3359
22. Ribeiro Jr. E., Regis W., Tasic L., and Ramos C. Fast purification of the Apo form and of a non-binding heme mutant of recombinant sperm whale myoglobin. Protein Expr. Purif. 28 (2003) 202-208
23. Tiroli A., Tasic L., Oliveira C., Bloch Jr. C., Torriani I., Farah C., and Ramos C. Mapping contacts between regulatory domains of skeletal muscule TnC and TnI by analyses of single-chain chimeras. FEBS 272 (2005) 779-790
24. Casals C., Miguel E., and Perez-Gill J. Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles. Biochem. J. 296 (1993) 585-593
25. Cavatorta P., Giovanelli S., Bobba A., Riccio P., Szabo A.G., and Quagliariello E. Myelin basic protein interaction with zinc and phosphate: fluorescence studies on the water-soluble form of the protein. Biophys. J. 66 (1994) 1174-1179
26. McCubbin W.D., Edery I., Altmann M., Sonenberg N., and Kay C.M. Circular dichroism and fluorescence studies on protein synthesis initiation factor elF-4E and two mutant forms from the yeast Saccharomyces cerevisiae. J. Biol. Chem. 263 (1998) 17663-17671
27. Russo A., and Brand L. A nanosecond time-resolved florescence study of recombinant human myelin basic protein. J. Fluoresc. 9 (2004) 333-342
28. Galán J., and Wolf-Watz H. Protein delivery into eukaryotic cells by type III secretion machines. Nature 444 (2006) 567-573
29. Borges J.C., and Ramos C.H.I. Spectroscopic and thermodynamic measurements of nucleoside-induced changes in the humane 70 kDa heat shock cognate protein. Arch. Biochem. Biophy. 452 (2006) 46-54
30. Mayer M., and Meyer B. Group epitope mapping by Saturation Transfer Difference NMR to identify segments of a ligand in direct contact with protein receptor. J. Am. Chem. Soc. 123 (2001) 6108-6117
31. McCoy M.A., Senior M.M., and Wyss D. Screening of protein Kinases by ATP-STD NMR Spectroscopy. J. Am. Chem. Soc. 127 (2005) 7978-7979
32. Peikert C., Seeger K., Bhat R.K., and Berger S. Determination of the binding specifity of the 12S subunit of the transcarboxylase by saturation transfer difference NMR. Org. Biomol. Chem. 12 (2004) 1777-1781
33. Peters T., Biet T., and Herfurth L. NMR methods for screening the binding of ligands to proteins-identification and characterization of bioactive ligands. In: Krishna N.R., and Berliner L.J. (Eds). Protein NMR for the Millennium (2006), Springel US, New York 287-315