Member of the polyhydroxyalkanoate family, is synthesized and accumula…

Member of the polyhydroxyalkanoate family, is synthesized and accumulated as stored intracellular compounds in the form of insoluble cytoplasmic granulesunder conditions of nutrient imbalance in several bacterial genera [14?6]. PHB was initially synthesized in the logarithmic phase and gradually degraded and utilized during sporulation in B. thuringiensis [17?9]. Navarro et al. [20] reported that a linear relationship exists between -endotoxin production and PHB accumulation, and a minimum PHB accumulation of 0.52 mg/L is required before the onset of -endotoxin production in B. thuringiensis subsp. kurstaki HD-73. In other words, PHB synthesis and degradation play critical roles in the highly efficient expression of ICP.Liu et al. Microb Cell Fact (2015) 14:Page 10 ofTable 2 The list of the proteins up-regulated when Cu2+ was addedAccession Description emPAI CK1 C3ER38 M4LAX0 C3CHP5 C3BZ34 C3CRL9 C3I208 M4L1B2 C3CM51 C3BX70 A0RHK1 C3CMC5 D5TTP0 D5TJY1 A0RKS3 D5TLE4 C3E6D6 C3BYJ8 C3CPV6 C3CDB7 K0FJZ8 C3E7X2 C3CMB9 Q631K2 F0PR22 C3ETX6 C3EKF4 K0FMV8 Uncharacterized protein Uncharacterized protein Small acid-soluble spore protein C5 3-Oxoacyl-[acyl-carrier-protein] synthase 2 Glyceraldehyde-3-phosphate dehydrogenase Spore coat protein w 30S ribosomal protein S11 Glutamine synthetase Mature parasite-infected erythrocyte surface antigen GTP-sensing transcriptional pleiotropic repressor CodY Stage V sporulation protein S PhaR protein Citrate synthase Enolase Homogentisate 1,2-dioxygenase Aldehyde dehydrogenase Uncharacterized protein Short chain enoyl-CoA hydratase Alkyl hydroperoxide reductase subunit C DNA-binding protein HU 3-hydroxybutyrate dehydrogenase (BDH) Spore coat protein E ATP-dependent Clp protease proteolytic subunit 2 Elongation factor G 30S ribosomal protein S6 Methylmalonate semialdehyde dehydrogenase [acylating] Butyryl-CoA dehydrogenase ND 0.10 0.47 0.11 0.24 0.10 0.23 0.20 0.06 0.16 0.54 0.15 0.13 0.09 0.18 0.65 0.10 0.20 0.30 0.27 0.17 0.43 0.29 0.11 0.27 0.26 0.05 Cu1 0.18 0.47 0.78 0.15 0.33 0.32 0.32 0.29 0.10 0.22 1.37 0.20 0.21 0.16 0.25 0.92 0.33 0.44 0.43 0.37 0.43 0.91 0.38 0.14 0.37 0.35 0.20 CK2 ND ND ND ND 0.04 0.10 0.15 0.08 0.06 0.05 0.78 0.15 0.10 0.09 0.09 0.38 0.21 0.20 0.19 0.17 0.11 0.65 0.21 0.05 0.37 0.20 0.11 Cu2 0.18 0.47 0.47 0.15 0.33 0.32 0.42 0.17 0.13 0.10 1.37 0.26 0.17 0.16 0.15 0.65 0.33 0.31 0.30 0.27 0.17 0.91 0.29 0.06 0.49 0.26 0.14 emPAI value ratio (Cu to CK) The first batch ?4.65 1.66 1.36 1.38 3.30 1.38 1.49 1.52 1.37 2.54 1.37 1.55 1.72 1.37 1.41 3.31 2.20 1.40 1.39 2.60 2.10 1.29 1.31 1.39 1.35 3.74 The second batch ????9.10 3.30 PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/16989806 2.79 2.08 2.06 2.05 1.76 1.75 1.72 1.72 1.72 1.69 1.58 1.57 1.57 1.56 1.54 1.39 1.38 1.34 1.30 1.28 1.BDH is a key enzyme in the reuse of PHB deposits. PHB degradation is initiated by the action of PHB depolymerase to release the monomer 3-hydroxybutyrate (3HB) [21?3]. Upregulation of BDH indicates increased reuse of PHB deposits in the stationary and decline phases, which provide more substances and energy for ICP synthesis. Both PHB accumulation and growth rate show wild-type levels during growth on ethylamine compounds. These results demonstrate that PhaR controls the acetyl-CoA Capecitabine flux to PHB in this methylotrophic bacterium [24]. Results of the present study show that Cu2+ caused upregulation of PhaR and BDH (Fig. 3), and brought about downregulation of environmental informationprocessing proteins, glycan biosynthesis, metabolism proteins (Fig. 8) and.