Proteomics

Dataset Information

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Comparative proteomic analysis for a bifunctional chorismate mutase/prephenate dehydratase in Acidovorax citrulli


ABSTRACT: - Identification of proteins whose expression was affected by a bifunctional chorismate mutase/prephenate dehydratase in Acidovorax citrulli str. KACC17005 - Shotgun proteomic analysis was used - Two strains were used with three biological replicates (total 6 samples). WT: the wild-type strain. 12G: a bifunctional chorismate mutase/prephenate dehydratase knockout mutant

INSTRUMENT(S): LTQ Velos

ORGANISM(S): Acidovorax Citrulli

SUBMITTER: Sang-Wook Han  

LAB HEAD: Sang-Wook Han

PROVIDER: PXD019444 | Pride | 2021-09-09

REPOSITORIES: Pride

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Publications

Putative Bifunctional Chorismate Mutase/Prephenate Dehydratase Contributes to the Virulence of <i>Acidovorax citrulli</i>.

Kim Minyoung M   Lee Jongchan J   Heo Lynn L   Han Sang-Wook SW  

Frontiers in plant science 20200925


<i>Acidovorax citrulli</i> (<i>Ac</i>) is a plant pathogenic bacterium that causes bacterial fruit blotch (BFB) in cucurbit crops. Despite its importance in the cucurbit industry, resistant cultivars/lines against BFB have not yet been identified. Therefore, there is a need to characterize the virulence factors/mechanisms in <i>Ac</i> to control the disease. Chorismate mutase, a key enzyme in the shikimate pathway, produces aromatic amino acids. Here, we report the functions of putative bifuncti  ...[more]

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