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Cite: NAR/gkaa742 2020



PUL General Information

Literature Information

PUL ID

PUL0579

PubMed

21488982, Mol Microbiol. 2011 Jun;80(6):1549-60. doi: 10.1111/j.1365-2958.2011.07664.x. Epub 2011 May 5.

Characterization method

microarray,qRT-PCR,Western Blot,immunoprecipitation

Genomic accession number

NC_002505.1

Nucelotide position range

1058502-1062895

Substrate

N-acetylglucosamine

Loci

VC_RS04905-VC_RS04915

Species

Vibrio cholerae/666

Degradation or Biosynthesis

degradation

Gene Name

Locus Tag

Protein ID

Gene Position

GenBank Contig Range

EC Number

- VC_RS04905 WP_001013120.1 0 - 1215 (-) NC_002505.1:1058502-1059717 -
nagA VC_RS04910 WP_000271133.1 1217 - 2354 (-) NC_002505.1:1059719-1060856 3.5.1.25
- VC_RS04915 WP_001023164.1 2822 - 4394 (+) NC_002505.1:1061324-1062896 -

Cluster number

1

Gene name

Gene position

Gene type

Found by CGCFinder?

- 1 - 1215 (-) TF: DBD-Pfam|MarR,DBD-SUPERFAMILY|0040517 No
nagA 1218 - 2354 (-) CAZyme: CE9 Yes
- 2823 - 4394 (+) TC: gnl|TC-DB|P09323|4.A.1.1.2 Yes

PUL ID

PUL0579

PubMed

21488982, Mol Microbiol. 2011 Jun;80(6):1549-60. doi: 10.1111/j.1365-2958.2011.07664.x. Epub 2011 May 5.

Title

Two gene clusters co-ordinate for a functional N-acetylglucosamine catabolic pathway in Vibrio cholerae.

Author

Ghosh S, Rao KH, Sengupta M, Bhattacharya SK, Datta A

Abstract

Pathogenic microorganisms like Vibrio cholerae are capable of adapting to diverse living conditions, especially when they transit from their environmental reservoirs to human host. V. cholerae attaches to N-acetylglucosamine (GlcNAc) residues in glycoproteins and lipids present in the intestinal epithelium and chitinous surface of zoo-phytoplanktons in the aquatic environment for its survival and colonization. GlcNAc utilization thus appears to be important for the pathogen to reach sufficient titres in the intestine for producing clinical symptoms of cholera. We report here the involvement of a second cluster of genes working in combination with the classical genes of GlcNAc catabolism, suggesting the occurrence of a novel variant of the process of biochemical conversion of GlcNAc to Fructose-6-phosphate as has been described in other organisms. Colonization was severely attenuated in mutants that were incapable of utilizing GlcNAc. It was also shown that N-acetylglucosamine specific repressor (NagC) performs a dual role - while the classical GlcNAc catabolic genes are under its negative control, the genes belonging to the second cluster are positively regulated by it. Further application of tandem affinity purification to NagC revealed its interaction with a novel partner. Our results provide a genetic program that probably enables V. cholerae to successfully utilize amino - sugars and also highlights a new mode of transcriptional regulation, not described in this organism.