Proteomics

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Protein ubiquitination in Aspergillus nidulans

ABSTRACT: Protein ubiquitination, an evolutionarily conserved post-translational modification process in eukaryotes, and plays an important role in many biological processes. Aspergillus nidulans, a model filamentous fungus, contributes to our understanding of cellular physiology, metabolism and genetics, but its ubiquitination remains widely unknown. In this study, the ubiquitination sites in the proteome of A. nidulans were identified using a highly sensitive mass spectrometry combined with immuno-affinity enrichment of ubiquitinated peptides. The 4816 ubiquitination sites were identified in 1913 ubiquitinated proteins, accounting for 18.1% of total proteins in A. nidulans. Bioinformatic analysis suggested that the ubiquitinated proteins are associated with a number of biological functions and display various sub-cellular localizations. Meanwhile, seven motifs were revealed from the ubiquitinated peptides, and significantly over-presented in different pathways. This study presents a first proteome-wide view of ubiquitination in filamentous fungi, and provides an initial framework for exploring the physiological role of lysine ubiquitination in filamentous fungi.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Aspergillus

TISSUE(S): Mycelium

SUBMITTER: Sheng-hua Ying  

LAB HEAD: Sheng-hua Ying

PROVIDER: PXD002299 | Pride | 2015-09-10

REPOSITORIES: Pride

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Publications

Qualitative ubiquitome unveils the potential significances of protein lysine ubiquitination in hyphal growth of Aspergillus nidulans.

Chu Xin-Ling XL   Feng Ming-Guang MG   Ying Sheng-Hua SH  

Current genetics 20150902 1

Protein ubiquitination is an evolutionarily conserved post-translational modification process in eukaryotes, and it plays an important role in many biological processes. Aspergillus nidulans, a model filamentous fungus, contributes to our understanding of cellular physiology, metabolism and genetics, but its ubiquitination is not completely revealed. In this study, the ubiquitination sites in the proteome of A. nidulans were identified using a highly sensitive mass spectrometry combined with imm  ...[more]

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