Lysine acetylproteome analysis suggests its roles in primary and secondary metabolism in Saccharopolyspora erythraea

Verfasser / Beitragende:
[Dan Huang, Zhi-Hai Li, Di You, Ying Zhou, Bang-Ce Ye]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/3(2015-02-01), 1399-1413
Format:
Artikel (online)
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024 7 0 |a 10.1007/s00253-014-6144-2  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-014-6144-2 
245 0 0 |a Lysine acetylproteome analysis suggests its roles in primary and secondary metabolism in Saccharopolyspora erythraea  |h [Elektronische Daten]  |c [Dan Huang, Zhi-Hai Li, Di You, Ying Zhou, Bang-Ce Ye] 
520 3 |a Lysine acetylation is a dynamic, reversible posttranslational modification that is known to play an important role in regulating the activity of many key enzymes in bacteria. Acetylproteome studies have been performed on some bacteria. However, until now, there have been no data on Actinomycetes, which are the major producers of therapeutic antibiotics. In this study, we investigated the first acetylproteome of the erythromycin-producing actinomycete Saccharopolyspora erythraea using a high-resolution mass spectrometry-based proteomics approach. Using immune-affinity isolation of acetyl-peptides with an anti-acetyllysine antibody followed by nano ultra performance liquid chromatography tandem mass spectroscopy (nanoUPLC-MS/MS) analysis, we identified 664 unique lysine-acetylated sites on 363 proteins. Acetylated proteins are involved in many biological processes such as protein synthesis, glycolysis/gluconeogenesis, citric acid (TCA) cycle, fatty acid metabolism, secondary metabolism, and the feeder metabolic pathways of erythromycin synthesis. We characterized the acetylproteome and analyzed in detail the impact of acetylation on diverse cellular functions according to Gene Ontology and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways. Four motif sequences surrounding the acetylation sites (KACH, KACY, KACXXXXR, and KACXXXXK) were found in the S. erythraea acetylproteome. These findings suggest that abundant lysine acetylation occurs in Actinomycetes, expand our current knowledge of the bacterial acetylproteome, and provide insight into the regulatory function of acetylation in primary and secondary metabolism. 
540 |a Springer-Verlag Berlin Heidelberg, 2014 
690 7 |a Protein acetylation  |2 nationallicence 
690 7 |a Acetylome  |2 nationallicence 
690 7 |a Saccharopolyspora erythraea  |2 nationallicence 
690 7 |a Posttranslational modification  |2 nationallicence 
690 7 |a Actinomycetes  |2 nationallicence 
700 1 |a Huang  |D Dan  |u Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China  |4 aut 
700 1 |a Li  |D Zhi-Hai  |u Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China  |4 aut 
700 1 |a You  |D Di  |u Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China  |4 aut 
700 1 |a Zhou  |D Ying  |u Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China  |4 aut 
700 1 |a Ye  |D Bang-Ce  |u Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/3(2015-02-01), 1399-1413  |x 0175-7598  |q 99:3<1399  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-014-6144-2  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00253-014-6144-2  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Huang  |D Dan  |u Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Li  |D Zhi-Hai  |u Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a You  |D Di  |u Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Zhou  |D Ying  |u Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Ye  |D Bang-Ce  |u Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/3(2015-02-01), 1399-1413  |x 0175-7598  |q 99:3<1399  |1 2015  |2 99  |o 253