Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.7/353
Título: LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2
Autor: Marques, João C.
Oh, Il Kyu
Ly, Daniel C.
Lamosa, Pedro
Ventura, M. Rita
Miller, Stephen T.
Xavier, Karina B.
Palavras-chave: cell – cell signaling
quorum quenching
bacterial communication
metabolic flux
Data: 30-Set-2014
Editora: National Academy of Sciences
Citação: João C. Marques, Il Kyu Oh, Daniel C. Ly, Pedro Lamosa, M. Rita Ventura, Stephen T. Miller, and Karina B. Xavier LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2 PNAS 2014 111 (39) 14235-14240; published ahead of print September 15, 2014, doi:10.1073/pnas.1408691111
Resumo: The quorum sensing signal autoinducer-2 (AI-2) regulates important bacterial behaviors, including biofilm formation and the production of virulence factors. Some bacteria, such as Escherichia coli, can quench the AI-2 signal produced by a variety of species present in the environment, and thus can influence AI-2-dependent bacterial behaviors. This process involves uptake of AI-2 via the Lsr transporter, followed by phosphorylation and consequent intracellular sequestration. Here we determine the metabolic fate of intracellular AI-2 by characterizing LsrF, the terminal protein in the Lsr AI-2 processing pathway. We identify the substrates of LsrF as 3-hydroxy-2,4-pentadione-5-phosphate (P-HPD, an isomer of AI-2-phosphate) and coenzyme A, determine the crystal structure of an LsrF catalytic mutant bound to P-HPD, and identify the reaction products. We show that LsrF catalyzes the transfer of an acetyl group from P-HPD to coenzyme A yielding dihydroxyacetone phosphate and acetyl-CoA, two key central metabolites. We further propose that LsrF, despite strong structural homology to aldolases, acts as a thiolase, an activity previously undescribed for this family of enzymes. With this work, we have fully characterized the biological pathway for AI-2 processing in E. coli, a pathway that can be used to quench AI-2 and control quorum-sensing-regulated bacterial behaviors.
Peer review: yes
URI: http://hdl.handle.net/10400.7/353
DOI: 10.1073/pnas.1408691111
10.1073/pnas.1408691111
Versão do Editor: http://www.pnas.org/content/111/39/14235.long
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