Temporal dynamics of the Saccharopolyspora erythraea phosphoproteome

Licona-Cassani, Cuauhtemoc, Lim, SooA, Marcellin, Esteban and Nielsen, Lars K. (2014) Temporal dynamics of the Saccharopolyspora erythraea phosphoproteome. Molecular and Cellular Proteomics, 13 5: 1219-1230. doi:10.1074/mcp.M113.033951


Author Licona-Cassani, Cuauhtemoc
Lim, SooA
Marcellin, Esteban
Nielsen, Lars K.
Title Temporal dynamics of the Saccharopolyspora erythraea phosphoproteome
Formatted title
Temporal dynamics of the Saccharopolyspora erythraea phosphoproteome
Journal name Molecular and Cellular Proteomics   Check publisher's open access policy
ISSN 1535-9476
1535-9484
Publication date 2014-05
Sub-type Article (original research)
DOI 10.1074/mcp.M113.033951
Open Access Status
Volume 13
Issue 5
Start page 1219
End page 1230
Total pages 12
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2015
Language eng
Formatted abstract
Actinomycetes undergo a dramatic reorganization of metabolic and cellular machinery during a brief period of growth arrest (“metabolic switch”) preceding mycelia differentiation and the onset of secondary metabolite biosynthesis. This study explores the role of phosphorylation in coordinating the metabolic switch in the industrial actinomycete Saccharopolyspora erythraea. A total of 109 phosphopeptides from 88 proteins were detected across a 150-h fermentation using open-profile two-dimensional LC-MS proteomics and TiO2 enrichment. Quantitative analysis of the phosphopeptides and their unphosphorylated cognates was possible for 20 pairs that also displayed constant total protein expression. Enzymes from central carbon metabolism such as putative acetyl-coenzyme A carboxylase, isocitrate lyase, and 2-oxoglutarate dehydrogenase changed dramatically in the degree of phosphorylation during the stationary phase, suggesting metabolic rearrangement for the reutilization of substrates and the production of polyketide precursors. In addition, an enzyme involved in cellular response to environmental stress, trypsin-like serine protease (SACE_6340/NC_009142_6216), decreased in phosphorylation during the growth arrest stage. More important, enzymes related to the regulation of protein synthesis underwent rapid phosphorylation changes during this stage. Whereas the degree of phosphorylation of ribonuclease Rne/Rng (SACE_1406/NC_009142_1388) increased during the metabolic switch, that of two ribosomal proteins, S6 (SACE_7351/NC_009142_7233) and S32 (SACE_6101/NC_009142_5981), dramatically decreased during this stage of the fermentation, supporting the hypothesis that ribosome subpopulations differentially regulate translation before and after the metabolic switch. Overall, we show the great potential of phosphoproteomic studies to explain microbial physiology and specifically provide evidence of dynamic protein phosphorylation events across the developmental cycle of actinomycetes.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
Australian Institute for Bioengineering and Nanotechnology Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 8 times in Thomson Reuters Web of Science Article | Citations
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Created: Tue, 25 Mar 2014, 13:15:22 EST by Mr Esteban Marcellin Saldana on behalf of Aust Institute for Bioengineering & Nanotechnology