Molecular analysis of condensation domain in non-ribosomal peptide synthetase (NRPS) gene of Ganoderma boninense

• Main Authors: Shokrollahi, Neda, Ho, Chai Ling, Mohd Zainudin, Nur Ain Izzati, Abdul Wahab, Mohd As'wad, Wong, Mui Yun
• Format: Conference or Workshop Item
• Language: English
• Published: Faculty of Agriculture, Universiti Putra Malaysia 2018
• Online Access: http://psasir.upm.edu.my/id/eprint/77380/1/8TH%20IAC%20%E2%80%93%206TH%20ISFA%202018-59.pdf; http://psasir.upm.edu.my/id/eprint/77380/

Non-ribosomal peptides (NRPs) are a class of secondary metabolites produced by bacteria and filamentous fungi. So far, most fungal NRPs have been characterized for ascomycetes and basidiomycetes. Non-ribosomal peptide synthethases (NRPSs) are large multi-modular enzymes which catalyze these compounds. A minimal module for incorporation of one amino acid into the growing peptide chain consists of an adenylation (A) domain, a thiolation (T) or peptidyl carrier protein (PCP) domain and a condensation (C) domain. The C domain is required for peptide bond formation. The detection of NRPS in Ganoderma boninense and its involvement in basal stem rot (BSR) disease progression in oil palm was detected in an earlier study. However, the precise molecular structure of NRPS remains largely unknown in G. boninense. In this study, we aimed to identify and characterize the NRPS gene in G. boninense strain Gb001 using PCR-based method and bioinformatics tools, ANTISMASH and AUGUSTUS software. The results of this study indicated that a 2000 nucleotides encoding C domain of NRPS gene was detected. BLAST X demonstrated the fragment consisted of AMP- binding and Condensation Super family domains. Further study on differential expression of NRPS transcript on infected oil palm may pave a way towards developing a diagnostic tool for early detection of BSR.