Proteome-wide analyses reveal diverse functions of acetylation proteins in Neurospora crassa.

Abstract:

:Quantitative acetyl-proteomics, a newly identified post-translational modification, is known to regulate transcriptional activity in different organisms. Neurospora crassa is a model ascomycete fungus maintained for biochemistry and molecular biology research; however, extensive studies of the functions of its acylation proteins have yet to be performed. In this study, using LC-MS/MS qualitative proteomics strategies, we identified 1909 modification sites on 940 proteins in N. crassa and analysed the functions of these proteins using GO enrichment, KEGG pathway, and subcellular location experiments. We classified the acetylation protein involvement in diverse pathways, and protein-protein interaction (PPI) network analysis further demonstrated that these proteins participate in diverse biological processes. In summary, our study comprehensively profiles the crosstalk of modified sites, and PPI among these proteins may form a complex network with both similar and distinct regulatory mechanisms, providing improved understanding of their biological functions in N. crassa. This article is protected by copyright. All rights reserved.

journal_name

Proteomics

journal_title

Proteomics

authors

Wang T,Guan W,Du Y,Xu Y,He Z,Zhang Y,Kang C,Wan X,Chi X,Sun K,Zhang X

doi

10.1002/pmic.202000212

subject

Has Abstract

pub_date

2021-01-24 00:00:00

pages

e2000212

eissn

1615-9853

issn

1615-9861

pub_type

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