2020 journal article
Comparative Proteomic Analysis of Wild Type and Mutant Lacking an SCF E3 Ligase F-Box Protein in Magnaporthe oryzae
JOURNAL OF PROTEOME RESEARCH, 19(9), 3761–3768.
MeSH headings : Ascomycota; F-Box Proteins / genetics; Fungal Proteins / genetics; Magnaporthe / metabolism; Proteomics; Ubiquitin-Protein Ligases / genetics
TL;DR:
A label-free quantitative global proteomics technique was used to probe the role of ubiquitination and phosphorylation in the mechanism of how E3 ligase regulates change in virulence of M. oryzae and greatly assist in the selection of future genes for functional studies and enabling mechanistic insight related to virulence.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: October 5, 2020
Magnaporthe oryzae (M. oryzae) is a pathogenic, filamentous fungus that is a primary cause of rice blast disease. The M. oryzae protein MGG_13065, SCF E3 Ubiquitin Ligase complex F-box protein has been identified as playing a crucial role in the infection process, specifically, as part of the ubiquitin mediated proteolysis pathway. Proteins targeted by MGG_13065 E3 ligase are first phosphorylated and then ubiquitinated by E3 ligase. In this study, we used a label-free quantitative global proteomics technique to probe the role of ubiquitination and phosphorylation in the mechanism of how E3 ligase regulates change in virulence of M. oryzae. To do this, we compared the WT M.oryzae 70-15 strain with a gene knock out (E3 ligase KO) strain. After applying a ≥ 5 normalized spectral count cut off, a total of 4,432 unique proteins were identified comprised of 4,360 and 4,372 in the WT and E3 ligase KO samples, respectively. Eighty proteins drastically increased in abundance while 65 proteins decreased in abundance in the E3 ligase KO strain. Fifty-nine proteins were identified only in the WT strain; 13 of which had both phosphorylation and ubiquitination post-translational modifications. Seventy-one proteins were revealed to be only in the E3 ligase KO strain; 23 having both phosphorylation and ubiquitination post-translational modifications. Several of these proteins were associated with key biological processes. These data greatly assist in the selection of future genes for functional studies and enabling mechanistic insight related to virulence.