Project Title

SIR2 DEACETYLASE ENZYME AND ITS POSSIBLE ROLE IN PATHOGEN INFECTION

Authors' Affiliations

Department of Biomedical Science and Department of Biological Sciences, East Tennessee State University, Johnson City, TN-37614

Location

RIPSHIN MTN. ROOM 130

Start Date

4-4-2018 1:00 PM

End Date

4-4-2018 1:15 PM

Name of Project's Faculty Sponsor

Dr. Dhirendra Kumar

Faculty Sponsor's Department

Biological Sciences

Type

Oral Presentation

Classification of First Author

Graduate Student-Doctoral

Project's Category

Natural Sciences

Abstract Text

Silent Information Regulator 2 (SIR2) have a phylogenetically conserved catalytic domain from bacteria to humans. It catalyzes NAD+ dependent deacetylase activity post-translationally on acetylated lysine residues present in the protein. Because SIR2 are NAD+ dependent, its activity gets influenced by the change in the level of NAD+. SIR2 is responsible for calorie restriction and increased replicative yeast lifespan. It breakdown high energy bond in nicotinamide adenine dinucleotide (NAD), and the synthesis of O-acetyl-ADP-ribose which is a novel product. Lysine de/acetylation of histone molecule plays a significant role in chromatin dynamics in eukaryotes, but little is known in term of non-histone molecule modification by SIR2 enzyme especially in the case of the plant. SIP-428 is one of the SABP2 interacting protein (SIP) that exhibit SIR2 deacetylase activity. SABP2 is one of the essential components of salicylic acid (SA) signaling pathway that converts inactive methyl salicylate (MeSA) to active SA to induce local as well as SAR. AtSRT2, an Arabidopsis homolog of SIP-428 negatively regulate the basal resistance. Although catalytic domain is conserved, functional divergence has been reported in the case of SIR2 homologs. Presence of acetylated lysine residue in many cellular and organellar proteins implicated the possible physiological and metabolic role of SIP-428. Our result demonstrated SIP-428 exhibited NAD+ dependent deacetylase activity, but its lysine residue found to be acetylated, which raises the possibility of a post-translation regulatory mechanism that modulates the activity of SIP-428. SIP-428 have non-histone substrate, the negative regulator of basal resistance, and SAR. To understand better about the role of SIP-428 in plant physiology how it plays a vital role in SABP2 signaling pathway we will be using transgenic tobacco plant with altered expression of SIP-428 (Silence and inducible overexpression). Verified T3 generation of silence line and T2 generation of overexpression were created. These transgenic plant will be used to answer the possible link between SIP-428 and SABP2 in response to pathogen infection.

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Apr 4th, 1:00 PM Apr 4th, 1:15 PM

SIR2 DEACETYLASE ENZYME AND ITS POSSIBLE ROLE IN PATHOGEN INFECTION

RIPSHIN MTN. ROOM 130

Silent Information Regulator 2 (SIR2) have a phylogenetically conserved catalytic domain from bacteria to humans. It catalyzes NAD+ dependent deacetylase activity post-translationally on acetylated lysine residues present in the protein. Because SIR2 are NAD+ dependent, its activity gets influenced by the change in the level of NAD+. SIR2 is responsible for calorie restriction and increased replicative yeast lifespan. It breakdown high energy bond in nicotinamide adenine dinucleotide (NAD), and the synthesis of O-acetyl-ADP-ribose which is a novel product. Lysine de/acetylation of histone molecule plays a significant role in chromatin dynamics in eukaryotes, but little is known in term of non-histone molecule modification by SIR2 enzyme especially in the case of the plant. SIP-428 is one of the SABP2 interacting protein (SIP) that exhibit SIR2 deacetylase activity. SABP2 is one of the essential components of salicylic acid (SA) signaling pathway that converts inactive methyl salicylate (MeSA) to active SA to induce local as well as SAR. AtSRT2, an Arabidopsis homolog of SIP-428 negatively regulate the basal resistance. Although catalytic domain is conserved, functional divergence has been reported in the case of SIR2 homologs. Presence of acetylated lysine residue in many cellular and organellar proteins implicated the possible physiological and metabolic role of SIP-428. Our result demonstrated SIP-428 exhibited NAD+ dependent deacetylase activity, but its lysine residue found to be acetylated, which raises the possibility of a post-translation regulatory mechanism that modulates the activity of SIP-428. SIP-428 have non-histone substrate, the negative regulator of basal resistance, and SAR. To understand better about the role of SIP-428 in plant physiology how it plays a vital role in SABP2 signaling pathway we will be using transgenic tobacco plant with altered expression of SIP-428 (Silence and inducible overexpression). Verified T3 generation of silence line and T2 generation of overexpression were created. These transgenic plant will be used to answer the possible link between SIP-428 and SABP2 in response to pathogen infection.