The critical role of partially exposed N-terminal valine residue in stabilizing GH10 xylanase from Bacillus sp.NG-27 under poly-extreme conditions

PLoS ONE

Volumn 3, Issue 8, 2008, Pages

  Bharadwaj, Amit ^a,b   Leelavathi, Sadhu ^a   Mazumdar Leighton, Sudeshma ^b   Ghosh, Amit ^c   Ramakumar, Suryanarayanarao ^d   Reddy, Vanga S ^a  

^a INTERNATIONAL CENTRE FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Italy)

^b UNIVERSITY OF DELHI   (India)

^c Koba Institutional Area   (India)

^d INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCINE; METHIONINE; PROTEINASE K; RECOMBINANT PROTEIN; RECOMBINANT XYLAN ENDO 1,3 BETA XYLOSIDASE; UNCLASSIFIED DRUG; VALINE; XYLAN ENDO 1,3 BETA XYLOSIDASE; BACTERIAL PROTEIN;

ALKALINITY; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BACILLUS; CIRCULAR DICHROISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; GENE DELETION; HIGH TEMPERATURE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; START CODON; THERMOSTABILITY; CHEMICAL STRUCTURE; CHEMISTRY; MASS SPECTROMETRY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN DENATURATION;

BACILLUS SP. NG-27;

AMINO ACID SEQUENCE; BACILLUS; BACTERIAL PROTEINS; CIRCULAR DICHROISM; ENDOPEPTIDASE K; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; VALINE; XYLAN ENDO-1,3-BETA-XYLOSIDASE;

EID: 51849137782     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0003063     Document Type: Article

References (28)

1. Alberti E, Consonni R, Zetta L (2003) Applications of NMR to thermostable proteins. Annual Report in NMR Spectroscopy 50: 121-161.
2. Matthews BW (1993) Structural and genetic analysis of protein stability. Anon Rev Biochem 62: 139-160.
3. Fersht AR, Serrano L (1993) Principles of protein stability derived from protein engineering experiments. Curr Opin Structuct Biol 3(1): 75-83.
4. Funahashi J, Tkano K, Yamagata Y, Yutani K (2000) Role of surface hydrophobic residues in the conformational stability of human lysozyme at three diferent positions. Biochemistry 39(47): 14448-14456.
5. Pakula AA, Sauer RT (1990) Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface. Nature 344(6264): 363-364.
6. Frigerio F, Margarit I, Nogarotto R, De Filippis V, Granch G (1996) Cumulative stabilizing effect of hydrophobic interactions on the surface of the neutral protease from Bacillus Subtilis. Protein Eng 9(5): 439-445.
7. Perl D, Mueller U, Heinemann U, Schmid FX (2000) Two exposed aminc acid residues confer thermostability on a cold shock protein. Nature 7(5): 380-383.
8. Russell RJM, Taylor GL (1995) Engineering thermostability: lessons from thermophilic proteins. Curr Opin Biotechnol 6: 370-374.
9. Shallom D, Shoham Y (2003) Microbial hemicellulases. Curr Opin Microbiol 6(3): 219-228.
10. Leelavathi S, Gupta N, Maiti S, Ghosh A, Reddy VS (2003) Overproduction of an alkali- and thermo-stable xylanase in tobacco chloroplasts and efficient recovery of the enzyme. molecular breeding 11: 59-67.
11. Gupta N, Reddy VS, Maiti S, Ghosh A (2000) Cloning, expression, and sequence analysis of the gene encoding die alkali-stable, thermostable, endoxylanase from alkalophilic, mesophilic Bacillus Sp. strain NG-27. Appl Environ Microbiol 66: 2631-2635.
12. Manikandan K, Bhardwaj A, Ghosh A, Reddy VS, Ramakumar S (2005) Crystallization and preliminary X-ray study of a family 10 alkalithermostable xylanase from alkalophific Bacillus sp. NG-27. Acta CrytallograpSect F Struct Biol Cryst Common 61: 747-749.
13. Manikandan K, Bhardwaj A, Gupta N, Lokanath NK, Ghosh A, et al. (2006) Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic, Bacillus sp. NG-27:Structural insights into alkalophilicity and implications for adaptation to polyextreme conditions. Protein Sci 15: 1951-1960.
14. Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-Pdb Viewer: an environment for the comparative protein modeling. Electrophoresis 18: 2714-2723.
15. Lee B, Vasmatzis G (1997) Stabilization of protein structures. Curr Opin Biotechnol 8(4):,423-428.
16. Shortle D, Stites WE, Meeker AK (1990) Contributions of the Large Hydrophobic Amino Acids to the Stability of Staphylococcal Nuclease. Biochemistry 29(35): 8033-8041.
17. Machius M, Declererck N, Huber R, Wiegand G (2003) kinetic stabilization of Bacillus Lichenifornfis alpha-amylase through inroduction of hydrophobic residues at the surface. J Biol chem 278(13): 11546-11553.
18. Xie H, Flint J, Vardakou M, Lakey JH, Lewis RJ, et al. (2006) Probing the Structurae Basis for the Difference in Thermostability Displayed by Family 10 Xylanases. J Mol Biol 360(1): 157-167.
19. Van den Burg B, Dijkstra BW, Vriend G, Van Der Vinne B, Venema G, et al. (1994) protein stabilization by hydrophobic interactions at the surface. Fur J Biochem 220: 981-985.
20. Manning M, Colon W (2004) structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and bias towards beta-sheet structure. Biochemistry 43(35): 11248-11254.
21. Mamo G, Delgado O, Martinez A, Mattiasson B, Kant RJ (2006) clonning, sequencing analysis and expression of a gene encoding an endoxylanase from Bacilus halodurans S7. Met Biotechnol 33: 149-159.
22. Chang P, Tsai WS, Tsai CL, Tseng MJ (2004) clonning and characterization of two themistable xylanases from an alkalophilic Bacillus firmus. Biochem Biophys Res Common 319(3): 1017-1025.
23. Nakasako M (1999) Large-scale networks of hydration water molecules around bovine beta-trypsin revealed by cryogenic X-ray crystal structure analysis. J Mol Biol 289(3): 547-564.
24. Goldenberg DP, Berget PB, King J (1982) Maturation of the tail spike endorhamnosidase of Salmonella phage P22. J Biol Chem 257(13): 7864-7871.
25. Ihsanawati KT, Kaneko T, Morokuma C, Yetsunami R, Sato T, et al. (2005) Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8. Proteins 61(4): 999-1009.
26. Markert Y, Köditz J, Mansfeld J, Arnold U, Ulbrich-Hofmann R (2001) Increased protcolytic resistance of ribonuclease A by protein engineering. Protein Eng 14(10): 791-796.
27. Bradford. MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing die principle of protein-dye binding. Anal Biochem 72: 248 254.
28. Laemmli UK (1970) Cleavage of structural proteins during die assembly of the head of bacteriophagr T4. Nature 227(5259): 680-685.