Back to Search
Start Over
A comprehensive examination of the lysine acetylation targets in paper mulberry based on proteomics analyses
- Source :
- PLoS ONE, Vol 16, Iss 3, p e0240947 (2021), PLoS ONE
- Publication Year :
- 2021
- Publisher :
- Public Library of Science (PLoS), 2021.
-
Abstract
- Rocky desertification is a bottleneck that reduces ecological and environmental security in karst areas. Paper mulberry, a unique deciduous tree, shows good performance in rocky desertification areas. Its resistance mechanisms are therefore of high interest. In this study, a lysine acetylation proteomics analysis of paper mulberry seedling leaves was conducted in combination with the purification of acetylated protein by high-precision nano LC-MS/MS. We identified a total of 7130 acetylation sites in 3179 proteins. Analysis of the modified sites showed a predominance of nine motifs. Six positively charged residues: lysine (K), arginine (R), and histidine (H), serine (S), threonine (T), and tyrosine (Y) occurred most frequently at the +1 position, phenylalanine (F) was both detected both upstream and downstream of the acetylated lysines; and the sequence logos showed a strong preference for lysine and arginine around acetylated lysines. Functional annotation revealed that the identified enzymes were mainly involved in translation, transcription, ribosomal structure and biological processes, showing that lysine acetylation can regulate various aspects of primary carbon and nitrogen metabolism and secondary metabolism. Acetylated proteins were enriched in the chloroplast, cytoplasm, and nucleus, and many stress response-related proteins were also discovered to be acetylated, including PAL, HSP70, and ERF. HSP70, an important protein involved in plant abiotic and disease stress responses, was identified in paper mulberry, although it is rarely found in woody plants. This may be further examined in research in other plants and could explain the good adaptation of paper mulberry to the karst environment. However, these hypotheses require further verification. Our data can provide a new starting point for the further analysis of the acetylation function in paper mulberry and other plants.
- Subjects :
- Proteomics
Chloroplasts
Lysine
Amino Acid Motifs
Enzyme Metabolism
Plant Science
Biochemistry
Serine
Tandem Mass Spectrometry
Nanotechnology
Threonine
Post-Translational Modification
Amino Acids
Photosynthesis
Enzyme Chemistry
Chromatography, High Pressure Liquid
Protein Metabolism
Multidisciplinary
Chemistry
Organic Compounds
Plant Biochemistry
Chemical Reactions
Acetylation
Physical Sciences
Amino Acid Analysis
Medicine
Basic Amino Acids
Cellular Structures and Organelles
Cellular Types
Research Article
Plant Cell Biology
Science
Protein domain
Research and Analysis Methods
Protein Domains
Plant Cells
HSP70 Heat-Shock Proteins
Secondary metabolism
Molecular Biology Techniques
Molecular Biology
Histidine
Phenylalanine Ammonia-Lyase
Molecular Biology Assays and Analysis Techniques
Organic Chemistry
Chemical Compounds
Biology and Life Sciences
Proteins
Cell Biology
Gene Ontology
Metabolism
Enzymology
Morus
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 16
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....88c4aa714ea9885fe5757bf810039b91