Three of four GlnR binding sites are essential for GlnR-Mediated activation of transcription of the amycolatopsis mediterranei nas Operon

Journal of Bacteriology

Volumn 195, Issue 11, 2013, Pages 2595-2602

  Wang, Ying ^a,b   Wang, Jing Zhi ^a   Shao, Zhi Hui ^a   Yuan, Hua ^a   Lu, Yin Hua ^a   Jiang, Wei Hong ^a   Zhaoa, Guo Ping ^a,b,c,d   Wanga, Jin ^a  

^a INSTITUTE OF PLANT PHYSIOLOGY AND ECOLOGY   (China)

^b FUDAN UNIVERSITY   (China)

^c CHINESE NATIONAL HUMAN GENOME CENTER AT SHANGHAI   (China)

^d CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BACTERIAL GENE; BACTERIUM; BINDING SITE; DNA FOOTPRINTING; DNA SEQUENCE; GENE MUTATION; GLNR GENE; IN VITRO STUDY; IN VIVO STUDY; NOCARDIA MEDITERRANEA; NONHUMAN; OPERON; PRIORITY JOURNAL; PROMOTER REGION; STREPTOMYCES COELICOLOR; TRANSCRIPTION INITIATION;

ACTINOMYCETALES; BACTERIAL PROTEINS; BASE SEQUENCE; BINDING SITES; DNA FOOTPRINTING; ELECTROPHORETIC MOBILITY SHIFT ASSAY; GENE EXPRESSION REGULATION, BACTERIAL; GENES, REPORTER; MOLECULAR SEQUENCE DATA; MUTATION; OPERON; PROMOTER REGIONS, GENETIC; RECOMBINANT PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, BACTERIAL; TRANS-ACTIVATORS; TRANSCRIPTIONAL ACTIVATION;

EID: 84877945964     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00182-13     Document Type: Article

References (36)

1. Chiao JS, Xia TH, Mei BG, Jin ZK, Gu WL. 1995. Rifamycin SV and related ansamycins. Biotechnology 28:477-498.
2. Stewart V. 1994. Regulation of nitrate and nitrite reductase synthesis in enterobacteria. Antonie Van Leeuwenhoek 66:37-45.
3. Shao Z, Gao J, Ding X, Wang J, Chiao J, Zhao G. 2011. Identification and functional analysis of a nitrate assimilation operon nasACKBDEF from Amycolatopsis mediterranei U32. Arch. Microbiol. 193:463-477.
4. Lin JT, Goldman BS, Stewart V. 1994. The nasFEDCBA operon for nitrate and nitrite assimilation in Klebsiella pneumoniae M5al. J. Bacteriol. 176:2551-2559.
5. Lin JT, Goldman BS, Stewart V. 1993. Structures of genes nasA and nasB, encoding assimilatory nitrate and nitrite reductases in Klebsiella pneumoniae M5al. J. Bacteriol. 175:2370-2378.
6. Wu Q, Stewart V. 1998. NasFED proteins mediate assimilatory nitrate and nitrite transport in Klebsiella oxytoca (pneumoniae) M5al. J. Bacteriol. 180:1311-1322.
7. Lin JT, Stewart V. 1998. Nitrate assimilation by bacteria. Adv. Microb. Physiol. 39:1-30.
8. Chai W, Stewart V. 1998. NasR, a novel RNA-binding protein, mediates nitrate-responsive transcription antitermination of the Klebsiella oxytoca M5al nasF operon leader in vitro. J. Mol. Biol. 283:339-351.
9. Chai W, Stewart V. 1999. RNA sequence requirements for NasRmediated, nitrate-responsive transcription antitermination of the Klebsiella oxytoca M5al nasF operon leader. J. Mol. Biol. 292:203-216.
10. Wu SQ, Chai W, Lin JT, Stewart V. 1999. General nitrogen regulation of nitrate assimilation regulatory gene nasR expression in Klebsiella oxytoca M5al. J. Bacteriol. 181:7274-7284.
11. Amin R, Reuther J, Bera A, Wohlleben W, Mast Y. 2012. A novel GlnR target gene, nnaR, is involved in nitrate/nitrite assimilation in Streptomyces coelicolor. Microbiology 158:1172-1182.
12. Fink D, Weissschuh N, Reuther J, Wohlleben W, Engels A. 2002. Two transcriptional regulators GlnR and GlnRII are involved in regulation of nitrogen metabolism in Streptomyces coelicolor A3(2). Mol. Microbiol. 46: 331-347.
13. Tiffert Y, Supra P, Wurm R, Wohlleben W, Wagner R, Reuther J. 2008. The Streptomyces coelicolor GlnR regulon: identification of new GlnR targets and evidence for a central role of GlnR in nitrogen metabolism in actinomycetes. Mol. Microbiol. 67:861-880.
14. Wang J, Zhao GP. 2009. GlnR positively regulates nasA transcription in Streptomyces coelicolor. Biochem. Biophys. Res. Commun. 386:77-81.
15. Malm S, Tiffert Y, Micklinghoff J, Schultze S, Joost I, Weber I, Horst S, Ackermann B, Schmidt M, Wohlleben W, Ehlers S, Geffers R, Reuther J, Bange FC. 2009. The roles of the nitrate reductase NarGHJI, the nitrite reductase NirBD and the response regulator GlnR in nitrate assimilation of Mycobacterium tuberculosis. Microbiology 155:1332-1339.
16. Amon J, Brau T, Grimrath A, Hanssler E, Hasselt K, Holler M, Jessberger N, Ott L, Szokol J, Titgemeyer F, Burkovski A. 2008. Nitrogen control in Mycobacterium smegmatis: nitrogen-dependent expression of ammonium transport and assimilation proteins depends on the OmpRtype regulator GlnR. J. Bacteriol. 190:7108-7116.
17. Yu H, Yao Y, Liu Y, Jiao R, Jiang W, Zhao GP. 2007. A complex role of Amycolatopsis mediterranei GlnR in nitrogen metabolism and related antibiotics production. Arch. Microbiol. 188:89-96.
18. Wang Y, Cen XF, Zhao GP, Wang J. 2012. Characterization of a new GlnR binding box in the promoter of amtB in Streptomyces coelicolor inferred a PhoP/GlnR competitive binding mechanism for transcriptional regulation of amtB. J. Bacteriol. 194:5237-5244.
19. Lewis RA, Shahi SK, Laing E, Bucca G, Efthimiou G, Bushell M, Smith CP. 2011. Genome-wide transcriptomic analysis of the response to nitrogen limitation in Streptomyces coelicolor A3(2). BMC Res. Notes 4:78. doi:10.1186/1756-0500-4-78.
20. Pullan ST, Chandra G, Bibb MJ, Merrick M. 2011. Genome-wide analysis of the role of GlnR in Streptomyces venezuelae provides new insights into global nitrogen regulation in actinomycetes. BMC Genomics 12:175. doi:10.1186/1471-2164-12-175.
21. Mejia A, Barrios-Gonzalez J, Viniegra-Gonzalez G. 1998. Overproduction of rifamycin B by Amycolatopsis mediterranei and its relationship with the toxic effect of barbital on growth. J. Antibiot. (Tokyo) 51:58-63.
22. Kieser T, Bibb MJ, Buttner MJ, Chater KF, Hopwood DA. 2000. Practical Streptomyces genetics. John Innes Foundation, Norwich, United Kingdom.
23. Okanishi M, Suzuki K, Umezawa H. 1974. Formation and reversion of Streptomycete protoplasts: cultural condition and morphological study. J. Gen. Microbiol. 80:389-400.
24. Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
25. Raibaud O, Schwartz M. 1984. Positive control of transcription initiation in bacteria. Annu. Rev. Genet. 18:173-206.
26. Leblanc B, Moss T. 1994. DNase I footprinting. Methods Mol. Biol. 30:1-10.
27. Yu H, Peng WT, Liu Y, Wu T, Yao YF, Cui MX, Jiang WH, Zhao GP. 2006. Identification and characterization of glnA promoter and its corre-sponding trans-regulatory protein GlnR in the rifamycin SV producing actinomycete, Amycolatopsis mediterranei U32. Acta Biochim. Biophys. Sin. (Shanghai) 38:831-843.
28. Sola-Landa A, Rodriguez-Garcia A, Amin R, Wohlleben W, Martin JF. 2013. Competition between the GlnR and PhoP regulators for the glnA and amtB promoters in Streptomyces coelicolor. Nucleic Acids Res. 41: 1767-1782.
29. Wang R, Mast Y, Wang J, Zhang W, Zhao G, Wohlleben W, Lu Y, Jiang W. 2013. Identification of two-component system AfsQ1/Q2 regulon and its cross-regulation with GlnR in Streptomyces coelicolor. Mol. Microbiol. 87:30-48.
30. Perez-Martin J, de Lorenzo V. 1997. Clues and consequences of DNA bending in transcription. Annu. Rev. Microbiol. 51:593-628.
31. Stragier P, Patte JC. 1983. Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. III. Nucleotide sequence and regulation of the lysR gene. J. Mol. Biol. 168:333-350.
32. Stragier P, Richaud F, Borne F, Patte JC. 1983. Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. I. Identification of a lysR gene encoding an activator of the lysA gene. J. Mol. Biol. 168:307-320.
33. Chugani SA, Parsek MR, Chakrabarty AM. 1998. Transcriptional repression mediated by LysR-type regulator CatR bound at multiple binding sites. J. Bacteriol. 180:2367-2372.
34. van Keulen G, Ridder AN, Dijkhuizen L, Meijer WG. 2003. Analysis of DNA binding and transcriptional activation by the LysR-type transcriptional regulator CbbR of Xanthobacter flavus. J. Bacteriol. 185:1245-1252.
35. Muraoka S, Okumura R, Ogawa N, Nonaka T, Miyashita K, Senda T. 2003. Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend. J. Mol. Biol. 328:555-566.
36. Maddocks SE, Oyston PC. 2008. Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins. Microbiology 154: 3609-3623.