Embryogenesis of gymnosperm plant is a complex,dynamic and multistage *** this study,the Chinese fir seeds were analyzed at six stages spanning important developmental phases. The proteome profiles of seed samples wer...
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Embryogenesis of gymnosperm plant is a complex,dynamic and multistage *** this study,the Chinese fir seeds were analyzed at six stages spanning important developmental phases. The proteome profiles of seed samples were analyzed using 2-D difference gel electrophoresis (DIGE).One hundred thirty-six protein spots differing in kinetics of appearance were subjected to LC-MS/MS and MALDI-TOE Mass spectrometry data were interpreted that identified 77 of them. Hierarchical cluster analysis of the 77 spots recognized three main developmental profiles. Functional annotation of the Chinese fir developing seed proteins revealed that PCD is a central process for seed development,which may be multiple programs to execute PCD process in Chinese fir *** were also identified involved in carbon metabolism,Met metabolism,energy production,protein storage,synthesis and stabilization,disease/defense,cytoskeleton protein and proteins related to embryo *** involved in carbon metabolism were higher expression at the early stages,which probably provide substrates for starch *** related to Met metabolism were accumulated at the later stages,which had key role in the building block for protein and polyamines and hormone ethylene and implicated seed development tending to mature. This study provides a reference map for seed development of Chinese fir and might serve as potential markers for specific stage of seed development.
The antimicrobial peptide ABP-dHC-cecropin A is a small cationic peptide with potent activity against a wide range of bacterial species. Evidence of antifungal activity has also been suggested;however, testing of this...
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The antimicrobial peptide ABP-dHC-cecropin A is a small cationic peptide with potent activity against a wide range of bacterial species. Evidence of antifungal activity has also been suggested;however, testing of this peptide has been limited due to the low expression of cecrop in proteins in Escherichia coli. To improve expression of this peptide in E. coli, ABP-dHC-cecropin A was cloned into a pSUMO vector and transformed into E. coli, resulting in the production of a pSUMO-ABP-dHC-cecropin A fusion protein. The soluble form of this protein was then purified by Ni-IDA chromatography, yielding a total of496-mg protein per liter of fermentation culture. The SUMO-ABP-dHC-cecropin A fusion protein was then cleaved using a SUMO protease and re-purified by Ni-IDA chromatography, yielding a total of 158-mg recombinant ABP-dHC-cecropin A per liter of fermentation culture at a purity of ≥94%, the highest yield reported to date. Antifungal activity assays performed using this purified recombinant peptide revealed strong antifungal activity against both Candida albicans and Neurospora crassa, as well as Rhi-zopus, Fusarium, Alternaria, and Mucor species. Combined with previous analyses demonstrating strong antibacterial activity against a number of important bacterial pathogens, these results confirm the use of ABP-dHC-cecropin A as a broad-spectrum antimicrobial peptide, with significant therapeutic potential.
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