Analysis of the multicopper oxidase gene regulatory network of Aeromonas hydrophila

Abstract

Multicopper oxidase (MCO) is an enzyme which involves in reducing the oxygen in a four electron reduction to water with concomitant one electron oxidation of reducing the substrate. We have generated the 3-D structure of MCO by homology modeling and validated on the basis of free energy while 90.4 % amino acid residues present in allowed regions of Ramachandran plot. The screening of potential hazardous aromatic compounds for MCO was performed using molecular docking. We obtained Sulfonaphthal, Thymolphthalein, Bromocresol green and Phloretin derivatives of phenol and aromatic hydrocarbon were efficient substrates for MCO. The phylogeny of MCO reveals that other bacteria restrain the homologous gene of MCO may play an important role in biodegradation of aromatic compounds. We have demonstrated the gene regulatory network of MCO with other cellular proteins which play a key role in gene regulation. These findings provide a new insight for oxidization of phenolic and aromatic compounds using biodegradation process for controlling environmental pollution.

MOLECULAR STUDY OF Aeromonas hydrophila ISOLATED FROM STOOL SAMPLES IN NAJAF (IRAQ)

“…1-A gene of A. hydrophila isolates for 55 min at 100 Volt. Lane 1 Marker (1kb DNA ladder) Lane 5,6,7,8,9,11,12,13 were positive result isolates of A. hydrophila while 2,3,4 and 10 were negative result.…”

“…The PCR methods, have been developed for routine identification of the species of Aeromonasʼ most frequently involved in human disease [6] and to genetically detect putative virulence genes [7]. Molecular studies on Aeromonas species have received a little atten-tion in Iraq.…”

Comparative metatranscriptome analysis revealed broad response of microbial communities in two soil types, agriculture versus organic soil

“…also showed high expression in the M1 soil. Catalytic sites of these proteins contain copper-binding sites and are implicated in bacterial copper resistance, oxidation of phenolic compounds, and in detoxification of Mn 2+ [61]. Additionally, high expression of putative actin 22 in M1 indicates the formation of actin rods which was previously reported in Dictyostelium during the formation of spores under stress conditions such as heat shock and osmotic pressure as well as non-nutrient conditions [62, 63].…”

Molecular characterization and interactome analysis of aerolysin (aer) gene from fish pathogen Aeromonas veronii: The pathogenicity inferred from sequence divergence and linked to histidine kinase (cheA)

“…The studies on infection by A. hydrophilla reported a strong association between aer and cheA during bacterial signal transduction and chemotaxis (Seshadri et al, 2006;Singh, Mani, & Chaudhary, 2012;Wuethrich et al, 2014). However, the aer-cheA-mediated pathogenicity is yet to be studied in the case of A. veronii infection of fish.…”

“…Histidine kinase ( che A) is known to be associated with the pathogenicity of several human and animal infections including fish; however, the interactions between proteins are not precisely demonstrated in aquatic infections (Singh, Somvanshi, Rathore, Kapoor, & Mishra, ; Zhang, Ong, & Leung, ; Zhu, Li, Wang, Li, & Cai, ). The studies on infection by A. hydrophilla reported a strong association between aer and che A during bacterial signal transduction and chemotaxis (Seshadri et al, ; Singh, Mani, & Chaudhary, ; Wuethrich et al, ). However, the aer ‐ che A‐mediated pathogenicity is yet to be studied in the case of A. veronii infection of fish.…”