Structure and function of the Pseudomonas putida integration host factor

Journal of Bacteriology

Volumn 178, Issue 21, 1996, Pages 6319-6326

  Calb, Ron ^a   Davidovitch, Ayelet ^a   Koby, Simi ^a   Giladi, Hilla ^a   Goldenberg, Daniel ^a   Margalit, Hannah ^a   Holtel, Andreas ^b   Timmis, Kenneth ^b   Sanchez Romero, Juan Manual ^c,d   De Lorenzo, Victor ^c,d   Oppenheim, Amos B ^a  

^a HEBREW UNIVERSITY   (Israel)

^b HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

^c CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^d CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRATION HOST FACTOR;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DNA BINDING; GENE SEQUENCE; GENETIC ANALYSIS; MOLECULAR CLONING; NONHUMAN; OPERON; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN ANALYSIS; PROTEIN STRUCTURE; PSEUDOMONAS PUTIDA; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION;

ESCHERICHIA COLI; NEGIBACTERIA; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 10344229939     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.21.6319-6326.1996     Document Type: Article

References (39)

1. Abril, M. A., and J. L. Ramos. 1993. Physical organization of the upper pathway operon promoter of the Pseudomonas TOL plasmid. Sequence and positional requirements for XylR-dcpendent activation of transcription. Mol. Gen. Genet. 239:281-288.
2. 54-dependent Pu promoter of TOL plasmid. EMBO J. 10:1159-1167.
3. Drlica, K., and J. Rouviere-Yaniv. 1987. Histonelike proteins of bacteria. Microbiol. Rev. 51:301-319.
4. Fernandez, S., V. Shingler, and V. de Lorenzo. 1994. Cross-regulation by XylR and DmpR activators of Pseudomonas putida suggests that transcrip tional control of biodegradative operons evolves independently of catabolic genes. J. Bacteriol. 176:5052-5058.
5. Flamm, E. L., and R. A. Weisberg. 1985. Primary structure of the hip gene of Escherichia coli and of its product, the β subunit of integration host factor. J. Mol. Biol. 183:117-128.
6. Freundlich, M., N. Ramani, E. Mathew, A. Sirko, and P. Tsui. 1992. The role of integration host factor in gene expression in Escherichia coli. Mol. Microbiol. 6:2557-2563.
7. Friedman, D. I. 1988. Integration host factor: a protein for all reasons. Cell 55:545-554.
8. Gamas, P., A. C. Burger, G. Churcward, L. Caro, D. Galas, and M. Chandler. 1986. Replication of pSC101: effects of mutations in the E. coli protein IMF. Mol. Gen. Genet. 204:85-89.
9. L promoter at low temperature. Proc. Natl. Acad. Sci. USA 92:2184-2188.
10. Giladi, H., S. Koby, M. E. Gottesman, and A. B. Oppenheim. 1992. Supercoiling, integration host factor, and a dual promoter system, participate in the control of the bacteriophagc λ pL promoter. J. Mol. Biol. 224:937-948.
11. Gober, J. W., and L. Shapiro. 1990. Integration host factor is required for the activation of developmentally regulated genes in Caulobacter. Genes Dev. 4:1494-1504.
12. Granston, A. E., and H. A. Nash. 1993. Characterization of a set of integration host factor mutants deficient for DNA binding. J. Mol. Biol. 234:45-59.
13. Haluzi, H., D. Goitein, S. Koby, I. Mendelson, D. Teff, G. Mengeritsky, H. Giladi, and A. B. Oppenheim. 1991. Genes coding for integration host factor are conserved in gram-negative bacteria. J. Bacteriol. 173:6297-6299.
14. Holtel, A., S. Marques, I. Mohler, U. Jakubzik, and K. Timmis. 1994. Carbon source dependent inhibition of xyl operon expression of the Pseudomonas putida TOL plasmid. J. Bacteriol. 176:1173-1176.
15. Hoover, T. R., E. Santero, S. Porter, and S. Kustu. 1990. The integration host factor stimulates interaction of RNA polymerase with NIFA, the transcriptional activator for nitrogen fixation operons. Cell 63:11-22.
16. Karulis, P. 1991. MOLSCRIPT, computer graphics. J. Appl. Crystallogr. 24:946-950.
17. Lee, B., and F. M. Richards. 1971. The interpretation of protein structure: estimation of static accessibility. J. Mol. Biol. 55:379-400.
18. Lee, E. C., L. M. Hales, R. I. Gumport, and J. F. Gardner. 1992. The isolation and characterization of mutants of the integration host factor (IHF) of Escherichia coli with altered, expanded DNA-binding specificities. EMBO J. 11:305-313.
19. Lerner, C. G., and M. Inouye. 1990. Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white screening capability. Nucleic Acids Res. 18:4631.
20. 19a.Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harter, N.Y.
21. Marques, S., and J. Ramos. 1993. Transcriptional control of the Pseudomonus putida TOL plasmid catabolic pathways. Mol. Microbiol. 9:923-929.
22. Mengeritsky, G., D. Goldenberg, I. Mendelson, H. Giladi, and A. B. Oppenheim. 1993. Genetic and biochemical analysis of the integration host factor of Escherichia coli. J. Mol. Biol. 231:646-657.
23. Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
24. Oberto, J., K. Drlica, and J. Rouviere-Yaniv. 1994. Histones, HMG, HU, IHF: meme combat. Biochimie 76:901-908.
25. 54 dependent transcriptional activator of Pseudomonas putida. J. Mol. Biol. 258:575-587.
26. 54-dependent promoter Pu of the upper-TOL operon by intrinsically curved sequences. J. Biol. Chem. 269:1-6.
27. Short, J. M. 1988. λ ZAP: a bacteriophage λ expression vector with in vivo excision properties. Nucleic Acids Res. 15:7583-7600.
28. Stenzel, T. T., P. Patel, and D. Bastia. 1987. The integration host factor of Escherichia coli binds to bent DNA at the origin of replication of the plasmid pSC101. Cell 49:709-717.
29. Tanaka, I., K. Appelt, J. Dijk, S. W. White, and K. S. Wilson. 1984. 3-A resolution structure of a protein with histone-like properties in prokaryotes. Nature (London) 310:376-381.
30. Thompson, J. F., D. Waechter-Brulla, R. I. Gumport, J. F. Gardner, L. M. deVargas, and A. Landy. 1986. Mutations in an integration host factor-binding site: effect on lambda site-specific recombination and regulatory implications. J. Bacteriol. 168:1343-1351.
31. Toussaint, B., L. David, R. de Sury d'Aspermont, and P. M. Vignais. 1994. The IHF proteins of Rhodobacter capsulatus and Pseudomonas aeruginosa. Biochimie 76:951-957.
32. Toussaint, B., I. Delic-Attree, and P. M. Vignais. 1993. Pseudomonas aeruginosa contains an IHF-like protein that binds to the algD promoter. Biochem. Biophys. Res. Commun. 196:416-421.
33. Vis, H., M. Mariani, C. E. Vorgias, K. S. Wilson, R. Kaptein, and R. Boelens. 1995. Solution structure of the HU protein from Bacillus stearothermophilus. J. Mol. Biol. 254:692-703.
34. Weisberg, R. A., M. Freundlich, D. Friedman, J. Gardner, N. Goosen, H. Nash, A. Oppenheim, and J. Rouviere-Yaniv. 1996. Nomenclature of the genes encoding IHF. Mol. Microbiol. 19:642.
35. Werner, M. H., G. M. Clore, A. M. Gronenborn, and H. A. Nash. 1994. Symmetry and asymmetry in the function of Escherichia coli integration host factor: implication for target identification by DNA-binding proteins. Curr. Biol. 4:477-487.
36. White, S. W., K. Appelt, K. S. Wilson, and I. Tanaka. 1989. A protein structural motif that bends DNA. Proteins Struct. Funct. Genet. 5:281-288.
37. Wozniak, D. J., and D. E. Ohman. 1993. Involvement of the alginate algT gene and integration host factor in the regulation of the Pseudomonas aeruginosa algB gene. J. Bacteriol. 175:4145-4153.
38. Yang, C., and H. A. Nash. 1989. The interaction of E. coli IHF protein with its specific binding site. Cell 57:869-880.
39. Zulianello, L., E. de la Gorgue de Rosny, P. van Ulsen, P. van de Putte, and N. Goosen. 1994. The HimA and HimD subunits of integration host factor specifically bind to DNA as homodimers. EMBO J 13:1534-1540.