Please use this identifier to cite or link to this item: http://223.31.159.10:8080/jspui/handle/123456789/449
Title: Differential expression of peroxidase and ABC transporter as the key regulatory components for degradation of azo dyes by Penicillium oxalicum SAR-3
Authors: Saroj, Samta
Kumar, Karunesh
Prasad, Manoj
Singh, R. P.
Keywords: Quantitative real-time PCR
Suppression subtractive hybridization
Azo dye
Penicillium oxalicum
Bioremediation
Issue Date: 2014
Publisher: Springer
Citation: Funct. Integr. Genomics, 14(4): 631-642
Abstract: Fungal species are potential dye decomposers since these secrete spectra of extracellular enzymes involved in catabolism. However, cellular mechanisms underlying azo dye catalysis and detoxification are incompletely understood and obscure. A potential strain designated as Penicillium oxalicum SAR-3 demonstrated broad-spectrum catabolic ability of different azo dyes. A forward suppression subtractive hybridization (SSH) cDNA library of P. oxalicum SAR-3 constructed in presence and absence of azo dye Acid Red 183 resulted in identification of 183 unique expressed sequence tags (ESTs) which were functionally classified into 12 functional categories. A number of novel genes that affect specifically organic azo dye degradation were discovered. Although the ABC transporters and peroxidases emerged as prominent hot spot for azo dye detoxification, we also identified a number of proteins that are more proximally related to stress-responsive gene expression. Majority of the ESTs (29.5%) were grouped as hypothetical/unknown indicating the presence of putatively novel genes. Analysis of few ESTs through quantitative real-time reverse transcription polymerase chain reaction revealed their possible role in AR183 degradation. The ESTs identified in the SSH library provide a novel insight on the transcripts that are expressed in P. oxalicum strain SAR-3 in response to AR183.
Description: Accepted date: 21 September 2014
URI: http://172.16.0.77:8080/jspui/handle/123456789/449
ISSN: 1438-7948
Appears in Collections:Institutional Publications

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