Title |
COMPARATIVE ANALYSIS AND STRUCTURE ELUCIDATION OF SYNTAXIN- A NOVEL COMPONENT TENDS TO DEFENSE MECHANISM IN PLANT PROTEOMICS |
| J Plant Genom Vol:1 Iss:1 (2010-06-15) : 1-8 |
Authors |
Saurabh Shukla, Prashant Srivastava, Sanjay Kumar Choubey, Gomase V.S. |
Published on |
15 Jun 2010 Pages : 1-8 Article Id : BIA0001557 Views : 1009 Downloads : 866 |
DOI | http://dx.doi.org/10.9735/0976-8823.1.1.1-8 |
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Abstract |
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Syntaxin is one of the plants housekeeping resistance protein, occurred in most of the plants. Plants resist microbial attack using elaborate nonself surveillance systems consisting of a repertoire of cell surface and intracellular immune sensors. Thus plants must have evolved defense mechanisms to terminate extracellular colonization attempts. The plant must, therefore, promote an active resistance mechanism to combat the extracellular infection. Resistance against bacteria is manifested and whether similar processes mediate basal, gene for-gene, and salicylate-associated defense, however, so many resistant proteins are poorly understood. The influence of plasma membrane syntaxin is a component contributing to gene-for-gene resistance in Nicotiana benthamiana. Silencing the apparent orthologue of a syntaxin required for resistance to powdery mildew fungus, compromised resistance because syntaxins may play a role in secretion of proteins to the extracellular space, proteomic analysis of the apoplastic fluid. Syntaxin silenced plants were impaired in the accumulation of at least a subset of pathogenesisrelated (PR) proteins in the cell wall. SYP132-dependent secretion is a component of multiple forms of defense against bacterial pathogens in plants. Thus, we are implementing the Phylogenetics or comparative approach towards the syntaxin sequences observed in multiple plant genomes.
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Title |
PRODUCTION AND CHARACTERIZATION OF ALKALINE THERMOSTABLE PROTEASE FROM NEWLY ISOLATED BACILLUS SP. |
| J Plant Genom Vol:1 Iss:1 (2010-06-15) : 9-17 |
Authors |
Patil C.S., Gangawane A.K., Shankerappa S. Hatti |
Published on |
15 Jun 2010 Pages : 9-17 Article Id : BIA0001558 Views : 1029 Downloads : 932 |
DOI | http://dx.doi.org/10.9735/0976-8823.1.1.9-17 |
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Abstract |
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An inducible protease is produced by Bacillus sp. in undefined feather medium. Under submerged fermentation condition high level of protease production occurred at 45oC after 36 h at pH 10, with continuous agitation (180 rpm). The presence of carbon source in feather medium suppressed the enzyme production, while 0.1% yeast extract enhanced the production. The purified enzyme showed maximum protease activity at temperature 650C and at pH-10.The enzyme was monomeric and has molecular weight of approximately 66 kDa (SDS-PAGE).The enzyme may belong to serine protease group as it is completely inhibited by PMSF. Presence of metal ions such as Ca2+, Mg2+, Co2+, Ba2+ stimulated, while Hg2+, Pb2+, Zn2+, Fe2+ decreased the activity. The results indicate Bacillus sp. is a highly useful organism for feather meal production and in leather industry.
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