On January 30th 2020, the master student in Chemical Biology, Jinmin Liu, received from the NCCR Education Committee the Best Master’s Thesis Award 2020 for his work entitled: “Exploring tissue-specific responders of lipid-derived electrophiles in Caenorhabditis elegans”.
The prize implemented by the NCCR Chemical Biology acknowledges exceptional achievement of a young scientist enrolled in the Master in Chemical Biology programme at UNIGE. The work of Jinmin Liu has been selected on the basis of the following criteria: (1) great interdisciplinary value, (2) originality of the topic, (3) considerable research progress and maturity, (4) clarity of the written manuscript, (5) mastery of the domain as evidenced during the oral examination. He will receive a cash prize of CHF 2’000. The award also includes an invited special lecture on the occasion of the annual Retreat of the NCCR Chemical Biology in June 2020.
About his work
Posttranslational modifications (PTMs) play a crucial role in cellular signaling and communication. These modifications are classically created by enzymes. However, some PTMs form based on an intrinsically fast reaction between reactive small molecules and proteins. Of the latter class, non-enzyme mediated PTM by lipid-derived electrophiles (LDEs) is increasingly appreciated because of its high relevance to oxidative stress response and several diseases. Furthermore, the mechanism of many covalent drugs behaves similarly to LDE-protein interactions. Despite the importance of identifying LDE targets, relatively few sensor proteins showing the elevated reaction kinetics needed to serve as sensing proteins are known. Methods to identify these proteins in whole organisms, and with no intrinsic bias and importantly at tissue-specific levels with a high spatiotemporal resolution, are not well developed. Herein, we utilized genome-wide reactive electrophiles and oxidants (G-REX), a technique wherein a specific LDE is released transiently, at low concentration only in specific cell types to profile LDE responsive proteins in Caenorhabditis elegans. After enrichment of the locale-specific electrophile sensors, a tandem mass tag (TMT) labeling method was used to identify sensor proteins. Privileged protein sensors within five different cell types within the worm (all somatic cells, body-wall muscles, pharyngeal muscles, and intestine) were identified. Ubiquitin carboxyl-terminal hydrolase (Ubh-4), which is a cysteine protease, emerged as an important LDE sensor in all these cell types.