Salicylic acid binding protein 2 (SABP2) is one of the key enzymes in salicylic acid-dependent plant defense pathway. SABP2 is a 29 kDa protein present in extremely low abundance in plants and it catalyzes the conversion of signaling molecule methyl salicylate into salicylic acid. Although it has been shown that 6x His-tagged SABP2 over expressed in E. coli is a homodimer, its exact conformation in planta is still unknown. Therefore, we proposed to determine if SABP2 exist as a dimer and/or monomer under natural condition. To verify the exact conformation of native SABP2 protein in plant, SABP2 was purified from wild type tobacco using a 5-step purification protocol. Analysis of purified SABP2 in gel filtration and immunoblot assay suggested that SABP2 exists as a monomer in tobacco plant. Studies on SABP2 conformation will give us insight into the structure and functional relationship of this protein in salicylic acid-dependent disease resistance pathway.
| Identifer | oai:union.ndltd.org:ETSU/oai:dc.etsu.edu:etd-3615 |
| Date | 01 August 2011 |
| Creators | Hossain, Mir Ashad |
| Publisher | Digital Commons @ East Tennessee State University |
| Source Sets | East Tennessee State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Electronic Theses and Dissertations |
| Rights | Copyright by the authors. |
Page generated in 0.0017 seconds