Identification and characterization of two divergently transcribed iron regulated genes in Mycobacterium tuberculosis

Tubercle and Lung Disease

Volumn 79, Issue 5, 1999, Pages 287-298

  Marcela Rodriguez, G ^a,b   Gold, B ^a,b   Gomez, M ^a   Dussurget, O ^a,c   Smith, I ^a  

^a PUBLIC HEALTH RESEARCH INSTITUTE   (United States)

^b NEW YORK UNIVERSITY MEDICAL CENTER   (United States)

^c UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; HISTIDINE; IRON; MEMBRANE PROTEIN;

ARTICLE; BACTERIAL GENE; BINDING SITE; CONTROLLED STUDY; DNA FLANKING REGION; DNA FOOTPRINTING; GENE EXPRESSION; GENE FUSION; GENETIC TRANSCRIPTION; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OPEN READING FRAME; PRIORITY JOURNAL; PROMOTER REGION; REGULATOR GENE; REGULON;

MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

EID: 0032833150     PISSN: 09628479     EISSN: None     Source Type: Journal    
DOI: 10.1054/tuld.1999.0219     Document Type: Article

References (48)

1. Bullen J J, Rogers H J, Griffiths E. Role of iron in bacterial infection. Curr Top Microbiol Immunol. 80:1978;1-35.
2. Wheeler, P, R, Ratledge, C, Bloom, B, R, Tuberculosis. Pathogenesis, protection and control, ASM Press, Washington, DC, 353, 385.
3. Gobin J, Moore C H, Reeve J R, Wong D K, Gibson B W, Horwitz M A. Iron acquisition by Mycobacterium tuberculosis: Isolation and characterization of a family of iron-binding exochelins. Proc Natl Acad Sci USA. 92:1995;5189-5193.
4. Quadri L E, Keating J S A, Weinreb P H, Walsh C T. Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chemistry and Biology. 5:1998;631-645.
5. Gobin J, Horwitz M. Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall. J Experiment Med. 183:1996;1527-1532.
6. Clemens D L, Horwitz M A. The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin. J Exp Med. 184:1996;1349-1355.
7. Sturgill-Koszycki S, Schlesinger P H, Chakraborty P. Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase. Science. 263:1994;678.
8. Roweley D A, Halliwell B. Superoxide dependent formation of hydroxyl radical from NaDH and NADPH in the presence of iron salts. FEBS Letters. 142:1982;39-41.
9. Bagg A, Neilands J B. Molecular mechanism of regulation of siderophore-mediated iron assimilation. Microbiol Rev. 51:1987;509-518.
10. Litwin C M, Calderwood S B. Role of iron in regulation of virulence genes. Clin Microbiol Rev. 6:1993;137-149.
11. Tai S P S, Krafft A E, Nootheti P, Holmes R K. Coordinate regulation of siderophore and diphtheria toxin production by iron in Corynebacterium diphtheriae. Microb Pathog. 9:1990;267-273.
12. Doukhan L, Predich M, Nair G. Genomic organization of the mycobacterial sigma gene cluster. Gene. 165:1995;67-70.
13. Schmitt M P, Predich M, Doukhan L, Smith I, Holmes R K. Characterization of an iron-dependant regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae. Infect Immun. 63:1995;4284-4289.
14. Oguiza J A, Tao X, Marcos A T, Martin J F, Murphy J R. Molecular cloning, DNA sequence analysis, and characterization of the Corynebacterium diphtheriae dtxR homolog from Brevibacterium lactofermentum. J Bacteriol. 177:1995;465-467.
15. Gunter-Seeboth K, Schupp T. Cloning and sequence analysis of the Corynebacterium diptheriae dtxR homologue from Streptomyces lividans and Streptomyces pilosus encoding a putative iron repressor protein. Gene. 166:1995;117-119.
16. Dussurget O, Rodriguez G M, Smith I. An ideR mutant of Mycobacterium smegmatis has a derepressed siderophore production and an altered oxidative-stress response. Molecular Microbiol. 22:1996;535-544.
17. Fiss E H, Yu S, W R J Jr. Identification of genes involved in the sequestration of iron in mycobacteria: the ferric exochelin biosynthetic and uptake pathways. Molec Microbiol. 14:1994;557-569.
18. Dussurget, Gomez M, Timm J, Yu S, Jacobs W, Sabol S Z, Holmes R K, Smith I. Transcriptional control of the iron responsive fxbA gene by the mycobacterial regulator IdeR. J Bacteriol. 181:1998;3402-3408.
19. Dussurget O, Rodriguez G M, Smith I. Protective role of the mycobacterial IdeR against reactive oxygen species and isoniazid toxicity. Tuber Lung Dis. 79:1998;99-106.
20. Hall R M, Ratledge C. A simple method for the production of mycobactin, the lipid-soluble siderophore, from mycobacteria. FEMS Microbiol Lett. 15:1982;133-136.
21. Snapper S B, Melton R E, Mustapha S, Kieser T, Jacobs W. R. Jr. Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol Microbiol. 4:1990;1911-1919.
22. Connell N D. Mycobacterium: isolation, maintenance, transformation and mutant selection. 1994;Academic Press, San Diego.
23. Berghammer H, Auer B. Easypreps: fast and easy plasmid minipreparation for analysis of recombinant clones in Escherichia coli. BioTechniques. 14:1993;527-528.
24. Hamoen L W, Van Werkhove A F, Bijlsma J J, Dubnau D, Venema G. The competence transcription factor of Bacillus subtilis recognizes short A/T-rich sequences arranged in a unique, flexible pattern along the DNA helix. Genes Dev. 12:1998;1539-1550.
25. Gomez M, Nair G, Doukhan L, Smith I. sigA is an essential gene in Mycobacterium smegmatis. Molecular Microbiology. 29:1998;617-628.
26. Sambrook J, Fritsch E K, Maniatis T. Molecular cloning: a laboratory manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
27. Cutting S., Roels R, Losick R. Sporulation operon spolVF and the characterization of mutations that uncouple mother-cell from ferespore gene expression in Bacillis subtilis. J Mol Biol. 221:1991;1237-1256.
28. Miller J F. Experiments in molecular genetics. 1972;Cold spring Harbor Laboratory Press, Cold spring Harbor.
29. Schmitt M P, Holmes R K. Cloning, sequence, and footprint analysis of two promoter/operators from Corynebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and iron. J Bacteriol. 176:1994;1141-1149.
30. Lee J H, Wang T, Ault K, Liu J, Schmitt M P, Holmes R K. Identification and characterization of three new promoter/operators from Corynebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and iron. Infect Immun. 65:1997;4273-4280.
31. Tao X, Murphy J R. Determination of the minimal essential nucleotide sequence for diphtheria tox repressor binding by in vitro affinity selection. Proc Natl Acad Sci USA. 91:1994;9646-9650.
32. Altschul S F, Gish W, Miller W, Myers E W, Lipman D J. Basic alignment search tool. J Molecular Biology. 215:1990;403-410.
33. Winkler M E. Neidhardt F C. Escherichia coli and Salmonella. 1996;ASM press, Washington.
34. Cole S T, Brosch R, Parkhill J. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 393:1998;537-544.
35. Record T M Jr., Reznikoff W S, Craig M L, McQuade K L, Schlax P J. Neidhardt F C. Escherichia coli and Salmonella. Cellular and molecular biology. 1996;ASM Press, Washington.
36. Bashyam M D, Kaushal D, Dasgupta S K, Tyagi A K. A study of mycobacterial transcriptional apparatus identification of novel features in promoter elements. J Bacteriol. 178:1996;4847-4853.
37. Lee J H, Wang T, Ault K, Liu J, Schmitt M P, Holmes R. Identification and characterization of three new promoter/operators from Corynebacterium diphtheriae that are regulated by the Diphtheria toxin repressor (DtxR) and iron. Infect Immun. 65:1997;4273-4280.
38. White A, Ding X, vanderSpek J C, Murphy J R, Ringe D. Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex. Nature. 394:1998;502-506.
39. Limaur D, Avitabile A, Capelano C, Puglia A M, Bruni C B. Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2). Gene. 90:1990;31-41.
40. Fani R, Alfano P, Allota G, Bazzicalupo M, Carlomongo M S, Gallori E. The histidine operon of Azospirillium brasiliense: organization, nucleotide sequence and functional analysis. Res Microbiol. 144:1993;187-200.
41. Oriol E, Mendez-Alvarez S, Barbe J, Gilbert I. Cloning of the Rhodobacter sphaeroides hisE gene: unifunctionality of the encoded protein and lack of linkage to other his genes. Microbiology. 142:1996;2071-2078.
42. Hinshelwood S, Stoker N G. Cloning of mycobacterial histidine synthesis genes by complementation of a Mycobacterium smegmatis auxotroph. Molecular Microbiol. 6:1992;2887-2895.
43. Sharman G, Williams D, Ewing D, Ratledge C. Determination of the structure of exochelin MN, the extracellular siderophore of Mycobacterivrn neoaurum. Chemistry and Biology. 2:1995;553-561.
44. Hancock D H, Coxon B, Wang S, White E, Reeder E J, Bellama J M . L-Threo-B-hydroxyhistidine, an unprecedented iron(III) binding amino acid in a pyoverdin type siderophore fromPseudomonas fluorescens. J Chem Soc Chem Commun. 244:1993;468-470.
45. Tolmasky M E, Actis L A, Crosa J H. A histidine decarboxlase gene encoded by the Vibrio anguillarum plasmid pJM1 is essential for virulence: histamine is a precursor for the synthesis of anguibactin. Mol Microbiol. 15:1993;87-95.
46. Calder K M, Horwitz M A. Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding a low iron-induced protein and a metal transporting ATPase with similarities to two-component metal transport systems. Microb Pathog. 24:1998;133-143.
47. Wong D E, Lee B-Y, Horwitz M A, Gibson B W. Identification of Fur, aconitase and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentations of iron by combined two-dimensional gel electrophoresis and mass spectometry. Infect Immun. 67:1999;327-336.
48. Devereux J, Haeberli P, Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:1984;387-395.