Participation of Soluble Phophatidylserine Synthetase in Phosphatidylethanolamine Biosynthesis in <i>Escherichia coli</i> Membrane

Ishinaga, Masataka; Kito, Makoto

doi:10.1111/j.1432-1033.1974.tb03362.x

Cited by 27 publications

(13 citation statements)

References 18 publications

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“…The Amycolatopsis cell membrane belongs to the PII type because only one nitrogenous phospholipid, namely phosphatidyl ethanolamine (PE), was usually detected in its cell membrane [35]. In prokaryotes, phosphatidylserine is first generated from CDP-diacylglycerol, a general intermediate for the synthesis of different types of phospholipids, catalyzed by phosphatidylserine synthase (PssA, EC: 2.7.8.8), and is then transformed into PE [36, 37] by phosphatidylserine decarboxylase (Psd, EC: 4.1.1.65) (Figure 4A). Orthologs of both pssA (AORI_7346) and psd (AORI_7345) could be identified in the A. orientalis genome.…”

Section: Resultsmentioning

confidence: 99%

Complete genome sequence and comparative genomic analyses of the vancomycin-producing Amycolatopsis orientalis

Huang

Wei³

et al. 2014

BMC Genomics

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BackgroundAmycolatopsis orientalis is the type species of the genus and its industrial strain HCCB10007, derived from ATCC 43491, has been used for large-scale production of the vital antibiotic vancomycin. However, to date, neither the complete genomic sequence of this species nor a systemic characterization of the vancomycin biosynthesis cluster (vcm) has been reported. With only the whole genome sequence of Amycolatopsis mediterranei available, additional complete genomes of other species may facilitate intra-generic comparative analysis of the genus.ResultsThe complete genome of A. orientalis HCCB10007 comprises an 8,948,591-bp circular chromosome and a 33,499-bp dissociated plasmid. In total, 8,121 protein-coding sequences were predicted, and the species-specific genomic features of A. orientalis were analyzed in comparison with that of A. mediterranei. The common characteristics of Amycolatopsis genomes were revealed via intra- and inter-generic comparative genomic analyses within the domain of actinomycetes, and led directly to the development of sequence-based Amycolatopsis molecular chemotaxonomic characteristics (MCCs). The chromosomal core/quasi-core and non-core configurations of the A. orientalis and the A. mediterranei genome were analyzed reciprocally, with respect to further understanding both the discriminable criteria and the evolutionary implementation. In addition, 26 gene clusters related to secondary metabolism, including the 64-kb vcm cluster, were identified in the genome. Employing a customized PCR-targeting-based mutagenesis system along with the biochemical identification of vancomycin variants produced by the mutants, we were able to experimentally characterize a halogenase, a methyltransferase and two glycosyltransferases encoded in the vcm cluster. The broad substrate spectra characteristics of these modification enzymes were inferred.ConclusionsThis study not only extended the genetic knowledge of the genus Amycolatopsis and the biochemical knowledge of vcm-related post-assembly tailoring enzymes, but also developed methodology useful for in vivo studies in A. orientalis, which has been widely considered as a barrier in this field.Electronic supplementary materialThe online version of this article (doi:10.1186/1471-2164-15-363) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Complete genome sequence and comparative genomic analyses of the vancomycin-producing Amycolatopsis orientalis

Huang

Wei³

et al. 2014

BMC Genomics

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“…Phosphatidylethanolamine (PE) is a component of the lipid bilayer of the sarcoplasmic reticulum that promotes calcium binding to SERCA (17). PA, which is the product of DGK, is also the substrate for phosphatidylethanolamine biosynthesis (23). Thus, DGK haploinsufficiency may decreases SERCA activity by reducing PE levels.…”

Section: Discussionmentioning

confidence: 99%

Diacylglycerol kinase-δ regulates AMPK signaling, lipid metabolism, and skeletal muscle energetics

Jiang

Barbosa

Massart

et al. 2016

American Journal of Physiology-Endocrinology and Metabolism

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-Decrease of AMPK-related signal transduction and insufficient lipid oxidation contributes to the pathogenesis of obesity and type 2 diabetes. Previously, we identified that diacylglycerol kinase-␦ (DGK␦), an enzyme involved in triglyceride biosynthesis, is reduced in skeletal muscle from type 2 diabetic patients. Here, we tested the hypothesis that DGK␦ plays a role in maintaining appropriate AMPK action in skeletal muscle and energetic aspects of contraction. Voluntary running activity was reduced in DGK␦ ϩ/Ϫ mice, but glycogen content and mitochondrial markers were unaltered, suggesting that DGK␦ deficiency affects skeletal muscle energetics but not mitochondrial protein abundance. We next determined the role of DGK␦ in AMPK-related signal transduction and lipid metabolism in isolated skeletal muscle. AMPK activation and signaling were reduced in DGK␦ ϩ/Ϫ mice, concomitant with impaired lipid oxidation and elevated incorporation of free fatty acids into triglycerides. Strikingly, DGK␦ deficiency impaired work performance, as evident by altered force production and relaxation dynamics in response to repeated contractions. In conclusion, DGK␦ deficiency impairs AMPK signaling and lipid metabolism, thereby highlighting the deleterious role of excessive lipid metabolites in the development of peripheral insulin resistance and type 2 diabetes pathogenesis. DGK␦ deficiency also influences skeletal muscle energetics, which may lead to low physical activity levels in type 2 diabetes. lipid oxidation; skeletal muscle; diacylglycerol kinase; AMPK; contraction DIACYLGLYCEROL (DAG) KINASES (DGK) are a family of lipid kinases that catalyze the phosphorylation and conversion of DAG into phosphatidic acid (PA). Elevated DAG content is linked with the development of insulin resistance in type 2 diabetes (27, 36). Thus, modulating the level of distinct DGK isoforms may influence the level of DAG and consequently insulin sensitivity.DGKs regulate signal transduction via protein kinase C, Ras and Rho family proteins, and phosphatidylinositol 5-kinases (42). Of the ten different isoforms of mammalian DGKs, each may have a different subcellular localization and function (31). Protein abundance of DGK␦ and total DGK activity are reduced in skeletal muscle from type 2 diabetic patients and diabetic rodents and normalized upon correction of hyperglycemia (11). Given that DAG is a precursor for triglyceride biosynthesis, DGKs are potentially involved in regulating fat deposition. Indeed, DGK␦ haploinsufficient (DGK␦ ϩ/Ϫ ) mice develop obesity later in life (11), and knockdown of DGK␦ markedly suppresses triglyceride (TG) synthesis in 3T3-L1 preadipocytes (28). Yet, the mechanism by which DGK␦ affects lipid synthesis and other aspects of lipid metabolism remains unclear.AMP-activated protein kinase (AMPK) is a central regulator of energy metabolism. AMPK is heterotrimeric complex composed of a catalytic ␣-subunit and regulatory ␤-and ␥-subunits. Phosphorylation on the Thr 172 residue of ␣-subunit by liver kinase B (LKB1) (20) or calmo...

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“…The enzymes responsible for the biosynthcsis of phosphatidylglycerol from acyl-CoAs, sn-glycerol 3-phosphate and CTP (Scheme 1) are localized in the E. coli mcmbrane [4.27 -321, in contrast to phosphatidylethanolamine biosynthesis [29,30,32,33]. The major fatty acid species of E. coli phosphatidylglycerol are known to be palmitic, palmitoleic and cis-vaccenic acids.…”

Section: Biosjw Tlwsis Of'pkosylu7ti~~lgijcerol Molecular Species Bymentioning

confidence: 99%

Metabolism of the Phosphatidylglycerol Molecular Species in Escherichia coli

Kito

Ishinaga

Nishihara

et al. 1975

European Journal of Biochemistry

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The fractionation, turnover and biosynthesis of the phosphatidylglycerol molecular species of Escherichia coli were studied. Monoacetyldiglycerides derived from phosphatidylglycerol were separated into five subfractions; cis-vaccenyl-palmitoleyl, cis-vaccenyl-cis-vaccenyl, palmitylpalmitoleyl, palmityl-cis-vaccenyl and the disaturated molecular species on a silica gel plate impregnated with silver nitrate. Individual molecular species had different turnover rates. The palmityl-cisvaccenyl species was metabolized faster than the others. Disaturated species were rather stable. Various phosphatidylglycerol molecular species were synthesized in the presence of sn-glycerol 3-phosphate, palmityl-CoA, palmitoleyl-CoA, cis-vaccenyl-CoA and CTP by the E. coli membrane particulate fraction. When only the proportion of palmityl-CoA among the three acyl-CoAs was increased, the molecular species containing the palmityl residue were increased. Similar results were obtained with the other acyl-CoAs. However, a temperature-sensitive incorporation of unsaturated and saturated fatty acids into phosphatidylglycerol molecular species was observed with no change in the proportions of the three acyl-CoAs, completely reflecting the in vivo unsaturated/saturated ratio.We have reported [l-31 that differences in fatty acid composition were found among the major phospholipid classes of Escherichia coli, and that phosphatidylglycerol contained more cis-vaccenic acid than did phosphatidylethanolamine at any temperature. Hence, individual phospholipids appear to consist of different proportions of molecular species, which may control the membrane fluidity and phase separation. In contrast to phosphatidylethanolamine, phosphatidylglycerol plays a dynamic role in bacterial membranes. The rapid turnover of this phospholipid has been reported in E. coli [4-61. However, phosphatidylglycerol is required in the sugar transport process [7,8] and serves as a precursor of oligosaccharide [9]. No relationship has been established between the metabolic significance and variety of molecular species.The present paper deals with the separation, turnover and biosynthesis of the phosphatidylglycerol molecular species of E. coli.

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Participation of Soluble Phophatidylserine Synthetase in Phosphatidylethanolamine Biosynthesis in Escherichia coli Membrane

Cited by 27 publications

References 18 publications

Complete genome sequence and comparative genomic analyses of the vancomycin-producing Amycolatopsis orientalis

Complete genome sequence and comparative genomic analyses of the vancomycin-producing Amycolatopsis orientalis

Diacylglycerol kinase-δ regulates AMPK signaling, lipid metabolism, and skeletal muscle energetics

Metabolism of the Phosphatidylglycerol Molecular Species in Escherichia coli

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