Differences in malate dehydrogenases from the obligately piezophilic deep-sea bacterium Moritella sp. strain 2D2 and the psychrophilic bacterium Moritella sp. strain 5710

FEMS Microbiology Letters

Volumn 233, Issue 1, 2004, Pages 165-172

  Saito, Rie ^a   Nakayama, Akihiko ^a  

^a KINKI UNIVERSITY   (Japan)

Author keywords

Deep sea; Genus Moritella; Malate dehydrogenase; Obligately piezophilic bacterium; Psychrophilic bacterium

Indexed keywords

ALANINE; BACTERIAL ENZYME; GLUTAMINE; HISTIDINE; MALATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL GENE; BACTERIAL STRAIN; CONTROLLED STUDY; DEEP SEA; DNA SEQUENCE; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; GENE OVEREXPRESSION; GENE SEQUENCE; GENETIC VARIABILITY; HYDROSTATIC PRESSURE; HYPERBARISM; MOLECULAR CLONING; MORITELLA; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN LOCALIZATION; RESIDUE ANALYSIS; SEQUENCE HOMOLOGY; STRAIN DIFFERENCE; THERMOSTABILITY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CLONING, MOLECULAR; COLD; DNA, BACTERIAL; DNA, RIBOSOMAL; ENZYME STABILITY; ESCHERICHIA COLI; GENE EXPRESSION; GENES, BACTERIAL; GENES, RRNA; HYDROSTATIC PRESSURE; KINETICS; MALATE DEHYDROGENASE; MOLECULAR SEQUENCE DATA; MORITELLA; MUTAGENESIS, SITE-DIRECTED; MUTATION, MISSENSE; PHYLOGENY; RECOMBINANT PROTEINS; RNA, RIBOSOMAL, 16S; SEAWATER; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MORITELLA; MORITELLA SP.;

EID: 1642392368     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2004.02.004     Document Type: Article

References (29)

1. Somero G.N. Life at low volume change: hydrostatic pressure as a selective factor in the aquatic environment. Am. Zool. 30:1990;123-135.
2. Somero G.N. Adaptations to high hydrostatic pressure. Annu. Rev. Physiol. 54:1992;557-577.
3. Siebenaller J.F. Pressure adaptation in deep-sea animals. Jannasch H.W., Marquis R.E., Zimmerman A.M. Current Perspectives in High Pressure Biology. 1987;33-48 Academic Press, London.
4. Miyazaki K., Wintrode P.L., Grayling R.A., Rubingh D.N., Arnold F.H. Directed evolution study of temperature adaptation in a psychrophilic enzyme. J. Mol. Biol. 297:2000;1015-1026.
5. Feller G. Molecular adaptations to cold in psychrophilic enzymes. Cell. Mol. Life Sci. 60:2003;648-662.
6. Welch T.J., Bartlett D.H. Cloning, sequencing and overexpression of the gene encoding malate dehydrogenase from the deep-sea bacterium Photobacterium species strain SS9. Biochemi. Biophys. Acta. 1350:1997;41-46.
7. Nakayama A., Yano Y., Yoshida K. New method for isolating barophiles from intestinal contents of deep-sea fishes retrieved from the abyssal zone. Appl. Environ. Microbiol. 60:1994;4210-4212.
8. Hamamoto T., Takata N, Kudo T., Horikoshi K. Characteristic presence of polyunsaturated fatty acids in marine psychrophilic vibrios. FEMS Microbiol. Lett. 129:1995;51-56.
9. Ohkuma M., Ohtoko K., Takada N., Hamamoto T., Usami R., Kudo T., Horikoshi K. Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. strain no. 5710 and cloning of its gene. FEMS Microbiol. Lett. 137:1996;247-252.
10. Weisburg W.G., Barns S.M., Pelletier D.A., Lane D. 16S ribosomal DNA amplification for phylogenetic study. J. Bacteriol. 173:1991;697-703.
11. Lipman D.J., Pearson W.R. Rapid and sensitive protein similarity searches. Science. 227:1985;1435-1441.
12. Pearson W.R. Imported tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:1988;2444-2448.
13. Thompson J.D., Higgins D.G., Gibson T.J. Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
14. Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:1987;406-425.
15. Berns K.I., Thomas C.A. Jr. Isolation of high molecular weight DNA from Hemophilus influenzae. J. Mol. Biol. 11:1965;476-490.
16. Thomas C.A. Jr., Berns K.I., Kelly T.J. Jr. Isolation of high molecular weight DNA from bacteria and cell nuclei. Procedures in Nucleic Acid Research. vol. 1:1966;535-540 Harper & Row, New York.
17. McAlister-Henn L., Blaber M., Bradshow R.A., Nisco S.J. Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase. Nucleic Acids Res. 15:1987;4993.
18. Blattner F.R., Plunkett III G., Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. The complete genome sequence of Escherichia coli K-12. Science. 277:1997;1453-1462.
19. Urakawa H., Kita-Tsukamoto K., Steven S.E., Ohwada K., Colwell R.R. A proposal to transfer Vibrio marinus (Russell 1891) to a new genus Moritella gen. nov. as Moritella marina comb. nov. FEMS Microbiol. Lett. 165:1998;373-378.
20. Yanagibayashi M., Nogi Y., Li L., Kato C. Changes in the microbial community in Japan trench sediment from a depth of 6292 m during cultivation without decompression. FEMS Microbiol. Lett. 170:1999;271-279.
21. Kato C., Sato T., Horikoshi K. Isolation and properties of barophilic and barotolerant bacteria from deep-sea mud samples. Biodivers. Conserv. 4:1995;1-9.
22. Lunder T., Sørum H., Holstad G. Phenotypic and genotypic characterization of Vibrio viscosus sp. nov. and Vibrio wodanis sp. nov. isolated from Atrantic salmon (Salmo salar) with 'winter ulcer'. Int. J. Syst. Bacteriol. 50:2000;427-450.
23. Benediktsdóttir E., Verdonck L., Spröer C., Helgason S., Swings J. Characterization of Vibrio viscosus and Vibrio wodanis isolated at different geographical locations: a proposal for reclassification of Vibrio viscosus as Moritella viscosa comb. nov. Int. J. Syst. Evol. Microbiol. 50:2000;479-488.
24. Jeanmougin F., Thompson J.D., Gouy M., Higgins D.G., Gibson T.J. Multiple sequence alignment with Clustal X. Trends Biochem. Sci. 23:1998;403-405.
25. Roderick S.L., Banaszak L.J. The three-dimensional structure of porcine heart mitochondrial malate dehydrogenase at 3.0-Å resolution. J. Biol. Chem. 261:1986;9461-9464.
26. Birktoft J.J., Bradshaw R.A., Banaszak L.J. Structure of porcine heart cytoplasmic malate dehydrogenase: Combining X-ray diffraction and chemical sequence data in structural studies. Biochemistry. 26:1987;2722-2734.
27. Hall M.D., Levitt D.G., Banaszak L.J. Crystal structure of Escherichia coli malate dehydrogenase: a complex of the apoenzyme and citrate at 1.87 Å resolution. J. Mol. Biol. 226:1992;867-882.
28. Thompson L.M., Sutherland P., Steffan J.S., McAlister-Henn L. Gene sequence and primary structure of mitochondrial malate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 27:1988;8393-8400.
29. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.