Molecular analysis of condensation domain in non-ribosomal peptide synthetase (NRPS) gene of Ganoderma boninense
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 compound...
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| Format: | Conference or Workshop Item |
| Language: | English |
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Faculty of Agriculture, Universiti Putra Malaysia
2018
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| Online Access: | http://psasir.upm.edu.my/id/eprint/77380/1/8TH%20IAC%20%E2%80%93%206TH%20ISFA%202018-59.pdf |
| _version_ | 1825950842701742080 |
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| author | Shokrollahi, Neda Ho, Chai Ling Mohd Zainudin, Nur Ain Izzati Abdul Wahab, Mohd As'wad Wong, Mui Yun |
| author_facet | Shokrollahi, Neda Ho, Chai Ling Mohd Zainudin, Nur Ain Izzati Abdul Wahab, Mohd As'wad Wong, Mui Yun |
| author_sort | Shokrollahi, Neda |
| collection | UPM |
| description | 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. |
| first_indexed | 2024-03-06T10:20:48Z |
| format | Conference or Workshop Item |
| id | upm.eprints-77380 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T10:20:48Z |
| publishDate | 2018 |
| publisher | Faculty of Agriculture, Universiti Putra Malaysia |
| record_format | dspace |
| spelling | upm.eprints-773802020-03-05T06:30:03Z http://psasir.upm.edu.my/id/eprint/77380/ Molecular analysis of condensation domain in non-ribosomal peptide synthetase (NRPS) gene of Ganoderma boninense Shokrollahi, Neda Ho, Chai Ling Mohd Zainudin, Nur Ain Izzati Abdul Wahab, Mohd As'wad Wong, Mui Yun 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. Faculty of Agriculture, Universiti Putra Malaysia 2018 Conference or Workshop Item PeerReviewed text en http://psasir.upm.edu.my/id/eprint/77380/1/8TH%20IAC%20%E2%80%93%206TH%20ISFA%202018-59.pdf Shokrollahi, Neda and Ho, Chai Ling and Mohd Zainudin, Nur Ain Izzati and Abdul Wahab, Mohd As'wad and Wong, Mui Yun (2018) Molecular analysis of condensation domain in non-ribosomal peptide synthetase (NRPS) gene of Ganoderma boninense. In: Joint Symposium of the 8th International Agriculture Congress 2018 and 6th International Symposium for Food & Agriculture 2018 (8th IAC – 6th ISFA 2018), 13-15 Nov. 2018, Auditorium Rashdan Baba, TNCPI Building, Universiti Putra Malaysia. (pp. 294-296). |
| spellingShingle | Shokrollahi, Neda Ho, Chai Ling Mohd Zainudin, Nur Ain Izzati Abdul Wahab, Mohd As'wad Wong, Mui Yun Molecular analysis of condensation domain in non-ribosomal peptide synthetase (NRPS) gene of Ganoderma boninense |
| title | Molecular analysis of condensation domain in non-ribosomal peptide synthetase (NRPS) gene of Ganoderma boninense |
| title_full | Molecular analysis of condensation domain in non-ribosomal peptide synthetase (NRPS) gene of Ganoderma boninense |
| title_fullStr | Molecular analysis of condensation domain in non-ribosomal peptide synthetase (NRPS) gene of Ganoderma boninense |
| title_full_unstemmed | Molecular analysis of condensation domain in non-ribosomal peptide synthetase (NRPS) gene of Ganoderma boninense |
| title_short | Molecular analysis of condensation domain in non-ribosomal peptide synthetase (NRPS) gene of Ganoderma boninense |
| title_sort | molecular analysis of condensation domain in non ribosomal peptide synthetase nrps gene of ganoderma boninense |
| url | http://psasir.upm.edu.my/id/eprint/77380/1/8TH%20IAC%20%E2%80%93%206TH%20ISFA%202018-59.pdf |
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