AUTHOR=Ma Jin-Cheng , Wu Yun-Qi , Cao Dan , Zhang Wen-Bin , Wang Hai-Hong 

TITLE=Only Acyl Carrier Protein 1 (AcpP1) Functions in Pseudomonas aeruginosa Fatty Acid Synthesis

JOURNAL=Frontiers in Microbiology

VOLUME=8

YEAR=2017

URL=https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2017.02186

DOI=10.3389/fmicb.2017.02186

ISSN=1664-302X

ABSTRACT=<p>The genome of <italic>Pseudomonas aeruginosa</italic> contains three open reading frames, PA2966, PA1869, and PA3334, which encode putative acyl carrier proteins, AcpP1, AcpP2, and AcpP3, respectively. In this study, we found that, although these apo-ACPs were successfully phosphopantetheinylated by <italic>P. aeruginosa</italic> phosphopantetheinyl transferase (PcpS) and all holo-forms of these proteins could be acylated by <italic>Vibrio harveyi</italic> acyl-ACP synthetase (AasS), only AcpP1 could be used as a substrate for the synthesis of fatty acids, catalyzed by <italic>P. aeruginosa</italic> cell free extracts <italic>in vitro</italic>, and only <italic>acpP1</italic> gene could restore growth in the <italic>Escherichia coli</italic><italic>acpP</italic> mutant strain CY1877. And <italic>P. aeruginosa</italic><italic>acpP1</italic> could not be deleted, while disruption of <italic>acpP2</italic> or <italic>acpP3</italic> in the <italic>P. aeruginosa</italic> genome allowed mutant strains to grow as well as the wild type strain. These findings confirmed that only <italic>P. aeruginosa</italic> AcpP1 functions in fatty acid biosynthesis, and that <italic>acpP2</italic> and <italic>acpP3</italic> do not play roles in the fatty acid synthetic pathway. Moreover, disruption of <italic>acpP2</italic> and <italic>acpP3</italic> did not affect the ability of <italic>P. aeruginosa</italic> to produce <italic>N</italic>-acylhomoserine lactones (AHL), but replacement of <italic>P. aeruginosa</italic><italic>acpP1</italic> with <italic>E. coli</italic><italic>acpP</italic> caused <italic>P. aeruginosa</italic> to reduce the production of AHL molecules, which indicated that neither <italic>P. aeruginosa</italic> AcpP2 nor AcpP3 can act as a substrate for synthesis of AHL molecules <italic>in vivo</italic>. Furthermore, replacement of <italic>acpP1</italic> with <italic>E. coli</italic><italic>acpP</italic> reduced the ability of <italic>P. aeruginosa</italic> to produce some exo-products and abolished swarming motility in <italic>P. aeruginosa</italic>.</p>