Functional analysis of the RING type ubiquitin ligase family of Arabidopsis

Abstract

Protein ubiquitination plays an important role in various cellular processes. Protein modification by the attachment of ubiquitin regulates these processes by selectively targeting proteins for degradation by the proteasome. Ubiquitination also implicated in protein activation, endocytosis, and histone regulation. The ubiquitination pathway involves three key enzymes which attaches the small ubiquitin molecule to proteins. Of interest is the E3 ubiquitin ligase, which facilitates the transfer of ubiquitin to the substrate. The large number and different types of E3 lends to the specificity of this pathway. The purpose of this research is to characterize and analyze a sub-set Arabidopsis RING type E3 ligases so as to gain insight into how this modification is regulated and how it influence cellular responses. Very few Arabidopsis RING proteins have been studied therefore analysis to demonstrate activity and function of these proteins is of importance. My previous research focused on receptor kinase signaling by studying self-incompatibility in Brassica. In a broader sense, this work contributed to the understanding of flowering plant reproduction. The proposed research has broader implications in that it involves the functional characterization of a family of Arabidopsis proteins. This new area of research will serve to introduce me to the tools commonly used by Arabidopsis researchers but are not available to researchers utilizing other species such as Brassica. The RING E3s are predicted to be involved in many aspects of plant development, therefore this research will allow me to work on other areas of plant biology. The possibilities are endless.