Construction of a xylanase a variant capable of polymerization

PLoS ONE

Volumn 6, Issue 9, 2011, Pages

  Szabó, Veronika ^a   Muskotál, Adél ^a   Tóth, Balázs ^a,b   Mihovilovic, Marko D ^c   Vonderviszt, Ferenc ^a,d  

^a UNIVERSITY OF PANNONIA   (Hungary)

^b INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^c VIENNA UNIVERSITY OF TECHNOLOGY   (Austria)

^d INSTITUTE OF ENZYMOLOGY   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

FLAGELLIN; NANOMATERIAL; XYLAN ENDO 1,3 BETA XYLOSIDASE; ENDO 1,4 BETA XYLANASE; HYBRID PROTEIN;

ARTICLE; BACILLUS SUBTILIS; CATALYSIS; ENZYME ACTIVITY; GENETIC ENGINEERING; NONHUMAN; POLYMERIZATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; ENZYMOLOGY; GENETICS; METABOLISM;

BACTERIA (MICROORGANISMS);

BACILLUS SUBTILIS; ENDO-1,4-BETA XYLANASES; FLAGELLIN; RECOMBINANT FUSION PROTEINS;

EID: 80053098632     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025388     Document Type: Article

References (26)

1. Vonderviszt F, Namba K, (2008) Structure, function and assembly of flagellar axial proteins. In: Scheibel T, editors. Fibrous Proteins Landes Biosciences pp. 58-76.
2. Vonderviszt F, Kanto S, Aizawa SI, Namba K, (1989) Terminal regions of flagellin are disordered in solution. J Mol Biol 209: 127-133.
3. Minamino T, Imada K, Namba K, (2008) Mechanisms of type III protein export for bacterial flagellar assembly. Mol Biosyst 4: 1105-1115.
4. Yonekura K, Maki S, Morgan DG, DeRosier DJ, Vonderviszt F, et al. (2000) The bacterial flagellar cap as the rotary promoter of flagellin self-assembly. Science 290: 2148-2152.
5. Samatey FA, Imada K, Nagashima S, Vonderviszt F, Kumasaka T, et al. (2001) Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature 410: 331-337.
6. Yonekura K, Maki-Yonekura S, Namba K, (2003) Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424: 643-650.
7. Muskotál A, Seregélyes C, Sebestyén A, Vonderviszt F, (2010) Structural basis for stabilization of the hypervariable D3 domain of Salmonella flagellin upon filament formation. J Mol Biol 403: 607-615.
8. Henrissat B, Davies G, (1997) Structural and sequence-based classification of glycoside hydrolases. Curr Opin Struct Biol 7: 637-644.
9. Murakami MT, Arni RK, Vieira DS, Degreve L, Ruller R, et al. (2005) Correlation of temperature induced conformational change with optimum catalytic activity in the recombinant G/11 xylanase A from Bacillus subtilis strain 168 (1A1). FEBS Lett 579: 6505-6510.
10. Saijo-Hamano Y, Namba K, Oosawa K, (2000) A new purification method for overproduced proteins sensitive to endogenous proteases. J Struct Biol 132: 142-146.
11. Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins MR, et al. (2005) Protein identification and analysis tools on the ExPASy server. In: Walker JM, editors. The proteomics protocols handbook Humana Press, NJ pp. 571-607.
12. Bernfeld P, (1955) Amylases α and β. Methods Enzymol 1: 149-158.
13. Kim J, Grate JW, Wang P, (2008) Nanobiocatalysis and its potential applications. Trends Biotech 26: 639-646.
14. Ge J, Lu D, Liu Z, Liu Z, (2009) Recent advances in nanostructured biocatalysts. Biochem Eng J 44: 53-59.
15. Baxa U, Speransky V, Steven AC, Wickner RB, (2002) Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein. Proc Natl Acad Sci USA 99: 5253-5260.
16. Baldwin AJ, Bader R, Christodoulou J, MacPhee CE, Dobson CM, et al. (2006) Cytochrome display on amyloid fibrils. J Am Chem Soc 128: 2162-2163.
17. Vonderviszt F, Aizawa SI, Namba K, (1991) Role of the disordered terminal regions of flagellin in filament formation and stability. J Mol Biol 221: 1461-1474.
18. Mimori-Kiyosue Y, Vonderviszt F, Namba K, (1997) Locations of terminal segments of flagellin in the filament structure and their roles in polymerization and polymorphism. J Mol Biol 270: 222-237.
19. Mimori-Kiyosue Y, Vonderviszt F, Yamashita I, Fujiyoshi Y, Namba K, (1996) Direct interaction of flagellin termini essential for polymorphic ability of flagellar filament. Proc Natl Acad Sci USA 93: 15108-15113.
20. Stocker BA, Newton SM, (1994) Immune responses to epitopes inserted in Salmonella flagellin. Int Rev Immunol 11: 167-178.
21. Ezaki S, Tsukio M, Takagi M, Imanaka T, (1998) Display of heterologous gene products on the Eschericia coli cell surface as fusion proteins with flagellin. J Ferm Bioeng 5: 500-503.
22. Westerlund-Wikstrom B, (2000) Peptide display on bacterial flagella: principles and applications. Int J Med Microbiol 290: 223-230.
23. Kumara MT, Muralidharan S, Tripp BC, (2007) Generation and characterization of inorganic and organic nanotubes on bioengineered flagella of mesophilic bacteria. J Nanosci Nanotechnol 7: 2260-2272.
24. Woods RD, Takahashi N, Aslam A, Pleass RJ, Aizawa SI, et al. (2007) Bifunctional nanotube scaffolds for diverse ligands are purified simply from Eschericia coli strains coexpressing two functionalized flagellar genes. Nano Lett 7: 1809-1816.
25. Kumara MT, Tripp BC, Muralidharan S, (2007) Layer-by-layer assembly of bioengineered flagella protein nanotubes. Biomacromolecules 8: 3718-3722.
26. Kumara MT, Tripp BC, Muralidharan S, (2007) Exciton energy transfer in self-assembled quantum dots on bioengineered bacterial flagella nanotubes. J Phys Chem C 111: 5276-5280.