Features of dnaK operon genes of the obligate thermophile Bacillus thermoglucosidasius KP1006

Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology

Volumn 77, Issue 3, 2000, Pages 241-250

  Watanabe, Kunihiko ^a   Iwashiro, Teruhiko ^a   Suzuki, Yuzuru ^a  

^a KYOTO PREFECTURAL UNIVERSITY   (Japan)

Author keywords

Bacillus thermoglucosidasius; dnaK; Proline; Thermophile; Thermostability

Indexed keywords

BACTERIAL DNA; PROLINE; PROTEIN DNAK;

ARTICLE; BACILLUS; BACTERIAL GENE; CLONE; GENE OVEREXPRESSION; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; THERMOPHILIC BACTERIUM;

ADENOSINE TRIPHOSPHATASES; BACILLUS; BACTERIAL PROTEINS; CELL DIVISION; CLONING, MOLECULAR; DNA, BACTERIAL; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENES, BACTERIAL; GENOME, BACTERIAL; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; OPERON; PROLINE; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS, DNA;

EID: 0034060894     PISSN: 00036072     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1002483620374     Document Type: Article

References (31)

1. Ash C, Farrow JAE, Wallbanks S & Collins MD (1991) Phylogenic heterogeneity of the genus Bacillus revealed by comparative analysis of small-subunit-ribosomal RNA sequences. Lett. Appl. Microbiol. 13: 202-206
2. Asseldonk M, Simons A, Visser H, deVos W & Simons G (1993) Cloning, nucleotide sequence, and regulation analysis of the Lactococcus lactis dnaJ gene. J. Bacteriol. 175: 1637-1644
3. Bardwell JC & Craig EA (1984) Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proc. Natl. Acad. Sci. USA 81: 848-852
4. + gene. J. Biol. Chem. 261: 1782-1785
5. Blanc M, Marilley L, Beffa T & Aragno M (1997) Rapid identification of heterotrophic, thermophilic, spore-forming bacteria isolated from hot composts. Int. J. Syst. Bacteriol. 47: 1246-1248
6. Blum P, Velligan M, Lin N & Matin A (1992) DnaK-mediated alterations in human growth hormone protein inclusion bodies. Bio/Technology 10, 301-304
7. Buchberger A & Bukau B (1997) Escherichia coli DnaK. In: Geming M-J (Ed) Guidebook to Molecular Chaperones and Protein-Folding Catalysts (pp 22-25) Oxford University Press, New York
8. Hendrick JP, Langer T, Davis TA, Hartl FU & Wiedman M (1993) Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc. Natl. Acad. Sci. USA 90: 10216-10220
9. Herbort M, Schön U, Angermann K, Lang J & Schumann W (1996) Cloning and sequencing of the dnaK operon of Bacillus stearothermophilus. Gene 170: 81-84
10. Homuth G, Masuda S, Mogk A, Kobayashi Y & Schumann W (1997) The dnaK operon of Bacillus subtilis is heptacistronic. J. Bacteriol. 179: 1153-1164
11. Klostermeier D, Seidel R & Reinstein J (1998) Functional properties of the molecular chaperone DnaK from Thermus thermophilus. J. Mol. Biol. 279, 841-853
12. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
13. Lutkenhaus J & Addinall S G (1997) Bacterial cell division and the ring. Annu. Rev. Biochem. 66: 93-116
14. McCarty J & Walker G (1991) DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc. Natl. Acad. Sci. USA 88: 9513-9517
15. McCarty J & Walker G (1994) DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: expression of mutant DnaK proteins results in filamentation. J. Bacteriol. 176: 764-780
16. Motohashi K, Yohda M, Endo I & Yoshida M (1996) A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus. J. Biol. Chem. 271: 17343-17348
17. Narberhaus F, Giebeler K & Bahl H (1992) Molecular characterization of the dnaK gene region of Clostridium acetobutylicum, including grpE, dnaJ, and a new heat shock gene. J. Bacteriol. 174: 3290-3299
18. Paek KH & Walker G (1987) Escherichia coli null mutants are inviable at high temperature. J. Bacteriol. 169: 283-390
19. Sambrook J, Fritsch EF & Maniatis T (1989) Molecular Cloning: a Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
20. Shi W, Zhou Y, Wild J, Adler J & Gross CA (1992) DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli. J. Bacteriol. 174: 6256-6263
21. Suzuki Y (1989) A general principle of increasing protein thermostability. Proc. Jpn. Acad. Ser. B. Phy. Biol. Sci. 65: 146-148
22. Suzuki Y, Kishigami T & Abe S (1976) Production of extracellular α-glucosidase by a thermophilic Bacillus species. Appl. Environ. Microbiol. 31: 807-812
23. Suzuki Y, Kishigami T, Inoue K, Mizoguchi Y, Eto N, Takagi M & Abe S (1983) Bacillus thermoglucosidasius sp nov., a new species of obligately thermophilic bacilli. System. Appl. Microbiol. 4: 487-495
24. Vieira J & Messing J (1987) Production of single-stranded plasmid DNA. Methods Enzymol. 153: 3-11
25. Watanabe K & Suzuki Y (1998) Protein thermostabilization by proline substitutions. J. Mol. Catal. B Enzymatic 4: 167-180
26. Watanabe K, Iha H, Ohashi A, & Suzuki Y (1989) Cloning and expression in Escherichia coli of an extremely thermostable oligo-l,6-glucosidase gene from Bacillus thermoglucosidasius. J. Bacteriol. 171: 1219-1222
27. Watanabe K, Chishiro K, Kitamura K & Suzuki Y (1991) Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006. J. Biol. Chem. 266: 24287-24294
28. Watanabe K., Kitamura K. & Suzuki Y (1996) Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC7050 and the evolutionary consideration of proline residues. Appl. Environ. Microbiol. 62, 2066-2073
29. Watanabe K, Hata Y, Kizaki K, Katsube, Y & Suzuki Y (1997) The refined structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: structural characterization of proline substitution sites for protein thermostabilization. J. Mol. Biol. 269, 142-153
30. Wetzstein M, Völker U, Dedio J, Löbau S, Zuber U, Schiesswohl M, Herget C, Hecker M & Schumann W (1992) Cloning, sequencing and molecular analysis of the dnaK locus from Bacillus subtilis. J. Bacteriol. 174: 3300-3310
31. Yokoyama K, Kikuchi Y & Yasueda H (1998) Overexpression of DnaJ in Escherichia coli improves in vivo solubility of the recombinant fish-derived transglutaminase. Biosci. Biotechnol. Biochem. 62, 1205-1210