Quantitative Proteomics Analysis Confirmed Oxidative Metabolism Predominates inStreptomyces coelicolorversus Glycolytic Metabolism inStreptomyces lividans

Abstract

Recent physiological studies indicated that S. lividans metabolism was mainly glycolytic, whereas S. coelicolor metabolism was mainly oxidative. To determine whether such metabolic characteristics were correlated with consistent proteomics features, a comparative label-free, shotgun proteomics analysis of these strains was carried out. Among 2024 proteins identified, 360 showed significant differences in abundance between the strains. This study revealed that S. coelicolor catabolized glucose less actively than S. lividans, whereas the amino acids present in the medium were catabolized less actively by S. lividans than by S. coelicolor. The abundance of glycolytic proteins in S. lividans was consistent with its high glycolytic activity, whereas the abundance of proteins involved in the catabolism of amino acids in S. coelicolor provided an explanatory basis for its predominantly oxidative metabolism. In this study, conducted under conditions of low O2 availability, proteins involved in resistance to oxidative stress and those belonging to a DosR-like dormancy regulon were abundant in S. coelicolor, whereas tellurium resistance proteins were abundant in S. lividans. This indicated that the strains reacted differently to O2 limitation. Proteins belonging to the CDA, RED, and ACT pathways, usually highly expressed in S. coelicolor, were not detected under these conditions, whereas proteins of siderophores, 5-hydroxyectoine, and terpenoid biosynthetic pathways were present.

Comprehensive subcellular topologies of polypeptides in Streptomyces

“…Until now experimentally validated TAT substrates (31 proteins) [ 48 , 49 ], proteins detected in extracellular vesicles (26 proteins) [ 40 , 41 ] or in the exportome of S. lividans TK24 growing in MM–CAS medium (296 proteins) [ 71 ], have been presented. An additional comparative proteomics study between S. lividans and S. coelicolor growing under low O 2 conditions, detected 1832 proteins from which 1486 are cytoplasmic and 346 exported proteins [ 72 ].…”

Modeling Protein Destiny in Developing Fruit

“…Peptide ions were quantified based on extracted ion currents using the software MassChroQ (v2.2;Valot et al, 2011). Peptide intensities of each sample were normalized by using a method taking retention time into account, as described in Millan-Oropeza et al (2017). Before protein quantification, peptides shared by several proteins were removed.…”

Stress-Induced Expression is Enriched for Evolutionarily Young Genes in Diverse Budding Yeasts

“…Data filtering was set to peptide E-value < 0.05, protein log(E-value) < -2 and to a minimum of two identified peptides per protein. Relative quantification of protein abundance was carried out using two complementary methods, one based on spectral counting and other considering the area of eXtracted Ion Chromatograms (XIC) of a given peptide at specific retention time as described in Millan-Oropeza 2017 52 . MS data are available online on public databases via the PRIDE 53 repository with the dataset identifier PXD011426 and PROTICdb 51,54 or via the following URLs: http://moulon.inra.fr/protic/chassy_kluyveromyces http://moulon.inra.fr/protic/chassy_yarrowia http://moulon.inra.fr/protic/chassy_saccharomyces…”