Carboxyl-terminal processing of the cytoplasmic NAD-reducing hydrogenase of Alcaligenes eutrophus requires the hoxW gene product

Journal of Bacteriology

Volumn 178, Issue 8, 1996, Pages 2368-2374

  Thiemermann, Sven ^a   Dernedde, Jens ^a   Bernhard, Michael ^b   Schroeder, Werner ^a   Massanz, Christian ^b   Friedrich, Bärbel ^a,b  

^a FREIE UNIVERSITÄT BERLIN   (Germany)

^b HUMBOLDT UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN; HYDROGENASE; NICKEL;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; DELETION MUTANT; NONHUMAN; OPEN READING FRAME; OXIDATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROCESSING; STRUCTURAL GENE; WAUTERSIA EUTROPHA;

ALCALIGENES; WAUTERSIA EUTROPHA;

EID: 0030012735     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.8.2368-2374.1996     Document Type: Article

References (43)

1. Altschul, S. F., W. Gish, W. Miller, E. W. Meyers, and D. J. Lipman. 1990. Basic local alignment search tool J Mol. Biol. 215:403-410.
2. Anbudurai, P. R., T. S. Mor, I. Ohad, S. V. Shestakov, and H. B. Pakrasi. 1994. The ctpA gene encodes the c-terminal processing protease for the D1 protein of the photosystem II reaction center complex. Proc. Natl. Acad. Sci. USA 91:8082-8086.
3. Bernhard, M., J. Rietdorf, and B. Friedrich. Unpublished data.
4. Bowien, B., and H. G. Schlegel. 1981. Physiology and biochemistry of aerobic hydrogen-oxidizing bacteria. Annu. Rev. Microbiol. 35:405-452.
5. Dernedde, J., M. Eitinger, and B. Friedrich. 1993. Analysis of a pleiotropic gene region involved in formation of catalytically active hydrogenase in Alcaligenes eutrophus. Arch. Microbiol. 159:545-553.
6. Dernedde, J., T. Eitinger, N. Patenge, and B. Friedrich. 1996. hyp gene products in Alcaligenes eutrophus are part of a hydrogenase maturation system. Eur. J Biochem. 235:351-358.
7. Friedrich, B., and E. Schwartz. 1993 Molecular biology of hydrogen utilization in aerobic chemolithotrophs Annu. Rev Microbiol. 47:351-383.
8. Friedrich, C. G., B. Friedrich, and B. Bowien. 1981. Formation of enzymes of autotrophic metabolism during heterotrophic growth of A. eutrophus. J. Gen. Microbiol. 122:69-78.
9. Gollin, D. J., L. E. Mortenson, and R. L. Robson. 1992. Carboxyl-terminal processing may be essential for production of active NiFe hydrogenase in Azotobacter vinelandii. FEBS Lett. 309:371-375.
10. Gough, J., and N. Murray. 1983. Sequence diversity among related genes for recognition of specific targets in DNA molecules. J. Mol. Biol. 166:1-19.
11. Gross, E., and B. Witkop. 1961. Specific cleavage of methionyl peptides. J. Am. Chem. Soc. 83:1509-1511.
12. Knauf, V. C., and E. W. Nester. 1982. Wide host range cloning vectors: a cosmid clone bank of an Agrobacterium Ti plasmid. Plasmid 8:45-54.
13. Kortlüke, C., and B. Friedrich. 1992 Maturation of membrane-bound hydrogenase of Alcaligenes eutrophus H16 J. Bacteriol. 174:6290-6293
14. Kortlüke, C., C. Hogrefe, G. Eberz, A. Pühler, and B. Friedrich. 1987 Genes of lithoautotrophic metabolism are clustered on the megaplasmid pHG1 in Alcaligenes eutrophus Mol. Gen. Genet. 210:122-128.
15. Kortlüke, C., K. Horstmann, E. Schwartz, M. Rohde, R. Binsack, and B. Friedrich. 1992. A gene complex coding for the membrane-bound hydrogenase of Alcaligenes eutrophus H16 J Bacteriol. 174:6277-6289.
16. Laemmli, U. K. 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
17. Lambin, P., and J. M. Fine. 1979. Molecular weight estimation of proteins by electrophoresis in linear polyacrylamide gradient gels in absence of denaturing agents Anal. Biochem 98:160-168
18. Lenz, O., E. Schwartz, J. Dernedde, M. Eitinger, and B. Friedrich. 1994. The Alcaligenes eutrophus H16 hoxX gene participates in hydrogenase regulation. J Bacteriol. 176:4385-4393.
19. 1 Compounds, San Diego, Calif., 1995. Kluwer Academic Publishers. Dordrecht, The Netherlands, in press.
20. Mead, D. A., E. Szczesna-Skorupa, and B. Kemper. 1986. Single stranded DNA "blue" T7 promoter plasmids: a versatile tandem promoter system for cloning and engineering. Protein Eng 1:67-74.
21. Menon, N. K., J. Robbins, M. D. Vartanian, D. Patil, H. D. Peck, A. L. Menon, R. L. Robson, and A. E. Przybyla. 1993. Carboxy-terminal processing of the large subunit of NiFe hydrogenases FEBS Lett. 331:91-95.
22. Miller, J. H. 1972. Experiments in molecular genetics Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
23. Mobley, H. L. T., M. D. Island, and R. P. Hausinger. 1995. Molecular biology of microhial ureases. Microbiol. Rev 59:451-480.
24. Pappin, D. J. C., and J. B. C. Findlay. 1984. Sequence variability in the retinal-attachment domain of mammalian rhodopsins. Biochem. J. 217:605-613.
25. Rossmann, R., T. Maier, F. Lottspeich, and A. Böck. 1995. Characterisation of a protease from Escherichia coli involved in hydrogenase maturation. Eur. J. Biochem. 227:545-550.
26. Rossmann, R., M. Sauter, F. Lottspeich, and A. Böck. 1994. Maturation of the large subunit (HycE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-treminal processing at Arg537. Eur. J. Biochem 220:377-384.
27. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
28. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc Natl. Acad. Sci USA 74:5463-5467.
29. Sauter, M., R. Böhm, and A. Böck. 1992. Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli. Mol. Microbiol. 6:1523-1532.
30. Schink, B., and H. G. Schlegel. 1979. The membrane-bound hydrogenase of Alcaligenes eutrophus Solubilization, purification and biochemical properties. Biochim Biophys. Acta 567:315-324.
31. Schlegel, H. G., H. Kaltwasser, and G. Gottschalk. 1961. Ein Submersverfahren zur Kultur wasserstoffoxidierender Bakterien: Wachstumsphysiologische Untersuchungen. Arch. Mikrobiol. 38:315-324.
32. Schmitz, O., G. Boison, R. Hilscher, B. Hundeshagen, W. Zimmer, F. Lottspeich, and H. Bothe. 1995. Molecular biological analysis of a bidirectional hydrogenase from cyanobacteria. Eur. J. Biochem. 233:266-276.
33. Schneider, K., R. Cammack, and H. G. Schlegel. 1984. Content and localization of FMN, Fe-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca 1b. Eur. J. Biochem. 142:75-84.
34. Schneider, K., M. Pinkwart, and K. Jochim. 1983. Purification of hydrogenases by affinity chromatography on procion red-agarose. Biochem. J. 213: 391-398.
35. Schneider, K., and H. G. Schlegel. 1976. Purification and properties of the soluble hydrogenase from Alcaligenes eutrophus H16. Biochim. Biophys. Acta 452:66-80.
36. Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. Bio/Technology 1:717-743.
37. Sorgenfrei, O., D. Linder, M. Karas, and A. Klein. 1993. A novel very small subunit of a selenium containing [NiFe] hydrogenase of Methanococcus voltae is posttransiationally processed by cleavage at a defined position. Eur. J. Biochem 213:1355-1358.
38. Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA 76:4350-4354.
39. Tran-Betcke, A., U. Warnecke, C. Böcker, C. Zaborosch, and B. Friedrich. 1990. Cloning and nucleotide sequence of the genes for the subunits of the NAD-reducing hydrogenase of Alcaligenes eutrophus H16. J. Bacteriol. 172: 2920-2929
40. 2 uptake hydrogenases. Arch. Microbiol. 172:2920-2929.
41. Volbeda, A., M.-H. Charon, C. Piras, E. C. Hatchikian, M. Frey, and J. C. Fontecilla-Camps. 1995. Crystal structure of the nickel-iron hydrogenase from Desulfovibno gigas. Nature (London) 373:580-587.
42. Walker, J. E. 1992. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains Q. Rev. Biophys. 25:253-324.
43. Weidner, U., S. Geier, A. Ptock, T. Friedrich, H. Leif, and H. Weiss. 1993. The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli. J. Mol Biol. 233:109-122