Ubiquitination in Plant Meiosis: Recent Advances and High Throughput Methods

Abstract

Meiosis is a specialized cell division which is essential to sexual reproduction. The success of this highly ordered process involves the timely activation, interaction, movement, and removal of many proteins. Ubiquitination is an extraordinarily diverse post-translational modification with a regulatory role in almost all cellular processes. During meiosis, ubiquitin localizes to chromatin and the expression of genes related to ubiquitination appears to be enhanced. This may be due to extensive protein turnover mediated by proteasomal degradation. However, degradation is not the only substrate fate conferred by ubiquitination which may also mediate, for example, the activation of key transcription factors. In plant meiosis, the specific roles of several components of the ubiquitination cascade—particularly SCF complex proteins, the APC/C, and HEI10—have been partially characterized indicating diverse roles in chromosome segregation, recombination, and synapsis. Nonetheless, these components remain comparatively poorly understood to their counterparts in other processes and in other eukaryotes. In this review, we present an overview of our understanding of the role of ubiquitination in plant meiosis, highlighting recent advances, remaining challenges, and high throughput methods which may be used to overcome them.

Loss of E3 ligase HvST1 function substantially increases recombination

“…Ubiquitination of HvASY1 by HvST1 but not Hvst1 in vitro provides an indication that the lack of ZYP1 polymerization observed in Hvst1 may result from the loss of this post translational modification of ASY1, and potentially from other SC proteins. The ubiquitination cascade has a well-established and extensive role in meiotic progression across Eukaryota (45), and ubiquitin has been shown to localize to the chromosomal axes during meiotic prophase (47)(48). Osman, et al (49) previously identified proteasomal and ubiquitination related proteins in association with ASY1 in a pulldown from Brassica oleracea.…”

Targeting Inhibitor of Apoptosis Proteins to Overcome Chemotherapy Resistance—A Marriage between Targeted Therapy and Cytotoxic Chemotherapy

“…The IAPs can block caspase activation via two main mechanisms: they can act as enzyme blockers, blocking substrate entry into the caspase active domain, or target the caspases for proteasomal degradation via the process of ubiquitination [26]. Ubiquitination is an evolutionarily conserved process to promote the degradation of proteins tagged with the ubiquitin peptide [28]. In both mechanisms, the end result is a functional decrease in caspase activity and, thus, a greater degree of apoptosis inhibition.…”

Crossover interference mechanism: New lessons from plants

“…Late Pachytene stage). However, by which mechanism HEI10 can coarsen and how it is related to other ubiquitination processes during meiosis require further investigations (Orr et al, 2021;Ren et al, 2021). It is worth underlining that the analysis of pachytene bivalents using electron microscopy had already noticed different sizes and shapes of early (poorly interfering) versus late interfering 'recombination nodules' (RN) localize along the synaptonemal complex (Anderson and Stack, 2005).…”