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A thioesterase bypasses the requirement for exogenous fatty acids in the plsX deletion of Streptococcus pneumoniae.
Parsons, Joshua B; Frank, Matthew W; Eleveld, Marc J; Schalkwijk, Joost; Broussard, Tyler C; de Jonge, Marien I; Rock, Charles O.
Afiliação
  • Parsons JB; Department of Infectious Diseases, St. Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN, 38105, USA.
Mol Microbiol ; 96(1): 28-41, 2015 Apr.
Article em En | MEDLINE | ID: mdl-25534847
PlsX is an acyl-acyl carrier protein (ACP):phosphate transacylase that interconverts the two acyl donors in Gram-positive bacterial phospholipid synthesis. The deletion of plsX in Staphylococcus aureus results in a requirement for both exogenous fatty acids and de novo type II fatty acid biosynthesis. Deletion of plsX (SP0037) in Streptococcus pneumoniae did not result in an auxotrophic phenotype. The ΔplsX S. pneumoniae strain was refractory to myristic acid-dependent growth arrest, and unlike the wild-type strain, was susceptible to fatty acid synthesis inhibitors in the presence of exogenous oleate. The ΔplsX strain contained longer chain saturated fatty acids imparting a distinctly altered phospholipid molecular species profile. An elevated pool of 18- and 20-carbon saturated fatty acids was detected in the ΔplsX strain. A S. pneumoniae thioesterase (TesS, SP1408) hydrolyzed acyl-ACP in vitro, and the ΔtesS ΔplsX double knockout strain was a fatty acid auxotroph. Thus, the TesS thioesterase hydrolyzed the accumulating acyl-ACP in the ΔplsX strain to liberate fatty acids that were activated by fatty acid kinase to bypass a requirement for extracellular fatty acid. This work identifies tesS as the gene responsible for the difference in exogenous fatty acid growth requirement of the ΔplsX strains of S. aureus and S. pneumoniae.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Streptococcus pneumoniae / Tioléster Hidrolases / Proteínas de Bactérias / Deleção de Sequência / Ácidos Graxos Idioma: En Revista: Mol Microbiol Assunto da revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Streptococcus pneumoniae / Tioléster Hidrolases / Proteínas de Bactérias / Deleção de Sequência / Ácidos Graxos Idioma: En Revista: Mol Microbiol Assunto da revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Estados Unidos