» Articles » PMID: 8232213

Nopaline Causes a Conformational Change in the NocR Regulatory Protein-nocR Promoter Complex of Agrobacterium Tumefaciens Ti Plasmid PTiT37

Overview
Journal Mol Gen Genet
Date 1993 Oct 1
PMID 8232213
Citations 6
Authors
Affiliations
Soon will be listed here.
Abstract

The nocR gene of Agrobacterium tumefaciens Ti plasmid pTiT37 is the regulatory gene of the nopaline catabolism (noc) operon of pTiT37. We have cloned and sequenced nocR, which encodes a DNA-binding protein. The deduced amino acid sequence is similar to those of members of the LysR family of prokaryotic activator proteins. Gel retardation experiments demonstrated that the NocR protein binds to the nocR promoter in both the presence and absence of nopaline. The increased mobility of the complex and alterations in the DNase I footprints revealed a nopaline-induced conformational change in the NocR-DNA complex. Sequence analysis of the NocR binding site indicated the presence immediately downstream of the -10 sequence of the nocR promoter of a 12 bp putative operator overlapping a consensus gyrase recognition sequence and an 18 bp long alternating purine-pyrimidine sequence. These results suggest that nopaline-induced alterations in the NocR protein-nocR promoter complex might control gene expression in the noc operon.

Citing Articles

Detection of and response to signals involved in host-microbe interactions by plant-associated bacteria.

Brencic A, Winans S Microbiol Mol Biol Rev. 2005; 69(1):155-94.

PMID: 15755957 PMC: 1082791. DOI: 10.1128/MMBR.69.1.155-194.2005.


The trans-acting protein interacting with the DNA motif proximal to the transcriptional start site of plant L-asparaginase is bacterial sarcosine oxidase.

Jones W, Al-Samarrai T, Reeves J, Ryan G, Kirk C, Vincze E J Bacteriol. 2004; 186(3):811-7.

PMID: 14729708 PMC: 321473. DOI: 10.1128/JB.186.3.811-817.2004.


Ti plasmid-encoded octopine and nopaline catabolism in Agrobacterium: specificities of the LysR-type regulators OccR and NocR, and protein-induced DNA bending.

Kreusch D, von Lintig J, Schroder J Mol Gen Genet. 1995; 249(1):102-10.

PMID: 8552026 DOI: 10.1007/BF00290241.


The NocR repressor-activator protein regulates expression of the nocB and nocR genes of Agrobacterium tumefaciens.

Marincs F, White D Mol Gen Genet. 1994; 244(4):367-73.

PMID: 8078462 DOI: 10.1007/BF00286688.


Octopine and nopaline oxidases from Ti plasmids of Agrobacterium tumefaciens: molecular analysis, relationship, and functional characterization.

Zanker H, Lurz G, Langridge U, Langridge P, Kreusch D, Schroder J J Bacteriol. 1994; 176(15):4511-7.

PMID: 8045881 PMC: 196269. DOI: 10.1128/jb.176.15.4511-4517.1994.


References
1.
Frantz B, OHalloran T . DNA distortion accompanies transcriptional activation by the metal-responsive gene-regulatory protein MerR. Biochemistry. 1990; 29(20):4747-51. DOI: 10.1021/bi00472a001. View

2.
Hryniewicz M, KREDICH N . The cysP promoter of Salmonella typhimurium: characterization of two binding sites for CysB protein, studies of in vivo transcription initiation, and demonstration of the anti-inducer effects of thiosulfate. J Bacteriol. 1991; 173(18):5876-86. PMC: 208322. DOI: 10.1128/jb.173.18.5876-5886.1991. View

3.
Chang M, Crawford I . In vitro determination of the effect of indoleglycerol phosphate on the interaction of purified TrpI protein with its DNA-binding sites. J Bacteriol. 1991; 173(5):1590-7. PMC: 207307. DOI: 10.1128/jb.173.5.1590-1597.1991. View

4.
Chang M, Crawford I . The roles of indoleglycerol phosphate and the TrpI protein in the expression of trpBA from Pseudomonas aeruginosa. Nucleic Acids Res. 1990; 18(4):979-88. PMC: 330353. DOI: 10.1093/nar/18.4.979. View

5.
Kramer H, Niemoller M, Amouyal M, Revet B, Muller-Hill B . lac repressor forms loops with linear DNA carrying two suitably spaced lac operators. EMBO J. 1987; 6(5):1481-91. PMC: 553955. DOI: 10.1002/j.1460-2075.1987.tb02390.x. View