Sanjay Kapoor

Friday Seminar by Ms. Gautam Gawande

SK Lab/Friday/ January 12, 2018/ 3.30 pm/ Ubiquitin Proteasome pathway and its role in Anther Development.
Category: Research



Ubiquitin-proteasome pathway has become increasingly apparent during last decade. The general function of this pathway is to conjugate Ubiquitin to Lysine residues within the substrate proteins. These proteins are then targeted by 26S proteasome system and the former are then get degraded into smaller peptides. This conjugation of Ubiquitin to substrates are facilitated by the action of three enzymes: the ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2), and ubiquitin protein ligase (E3). The E1 forms a thioester bond with the C terminus of ubiquitin (Ub) in an ATP-dependent manner and transfers the activated Ub to an E2 enzyme. The E2 either transfers ubiquitin directly to the E3 in the case of HECT (for homology to E6-AP C terminus) E3s or binds the E3 and transfers the ubiquitin to the substrate.

In plants, regulated protein degradation by the Ubiquitin/26S proteasome contributes significantly to development by affecting a wide range of processes, including hormone signaling, embryogenesis, metabolism, senescence etc. Recent studies have shown that this pathway also plays a role in reproductive development of plants, like anther development right from its meiotic stages to the last stage i.e., anther dehiscence. With the advancement in sciences, roles of many Ubiquitin/26S proteasome pathway related genes that express specifically in anther developmental stages can be understood which will give new insights to this subject.