Degree Name
PhD (Doctor of Philosophy)
Program
Biomedical Sciences
Date of Award
12-2018
Committee Chair or Co-Chairs
Dhirendra Kumar
Committee Members
Cecilia A. McIntosh, Alok Agrawal, William L. Stone, and Antonio Rusinol
Abstract
SABP2 (Salicylic Acid Binding Protein 2) plays a vital role in the salicylic acid signaling pathway of plants both regarding basal resistance and systemic acquired resistance against pathogen infection. SIP-428 (SABP2 Interacting Protein-428) is a Silent information regulator 2 (SIR2) like deacetylase enzyme that physically interacts with SABP2 in a yeast two-hybrid interaction and confirmed independently by a GST pull-down assay. We demonstrated that SIP- 428 is an NAD+ dependent SIR2 deacetylase enzyme. Transgenic tobacco plants silenced in SIP- 428 expression via RNAi showed enhanced basal resistance to microbial pathogens. Moreover, these SIP-428-silenced lines also exhibited a robust induction of systemic acquired resistance. In contrast, the transgenic tobacco lines overexpressing SIP-428 showed compromised basal resistance and failed to induce systemic acquired resistance. These results indicate that SIP-428 is likely a negative regulator of SA-mediated plant immunity. Experiments using a SABP2 inhibitor showed that SIP-428 likely functions upstream of SABP2 in the salicylic acid signaling pathway. It also indicates that SABP2 is dependent on SIP-428 for its role in the SA signaling pathway. Subcellular localization studies using confocal microscopy and subcellular fractionation showed that SIP-428 localized in the mitochondria. These results clearly show a role for SIP-428 in plant immunity.
Document Type
Dissertation - unrestricted
Recommended Citation
Thakuri, Bal Krishna Chand, "SIP-428, a SIR2 Deacetylase Enzyme and Its Role in Biotic Stress Signaling Pathway" (2018). Electronic Theses and Dissertations. Paper 3505. https://dc.etsu.edu/etd/3505
Copyright
Copyright by the authors.
Included in
Biochemistry Commons, Biology Commons, Molecular Biology Commons, Molecular Genetics Commons, Plant Sciences Commons