The FabA-FabB Pathway Is Not Essential for Unsaturated Fatty Acid Synthesis but Modulates Diffusible Signal Factor Synthesis in <i>Xanthomonas campestris</i> pv. <i>campestris</i>

Yu, Yonghong; Cheng, Chin‐Hsiang; Jianrong, Ma; Zhang, Yuanyin; Yan, Ming; Zhang, Wenbin; Hu, Zhe; Wang, Haihong; Ma, Jincheng

doi:10.1094/mpmi-09-22-0182-r

Cited by 4 publications

(3 citation statements)

References 56 publications

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“…At the transcriptome level, DSF biosynthesis is overproduced in the presence of the rpfC deletion and is reduced in the presence of overexpression of the REC domain [ 44 ]. The REC domain blocks the putative substrate from binding to the Lock RpfF protein in an inactive state; thus, RpfC negatively controls DSF production [ 51 ].…”

Section: Dsf Biosynthasementioning

confidence: 99%

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Research on Diffusible Signal Factor-Mediated Quorum Sensing in Xanthomonas: A Mini-Review

et al. 2023

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Xanthomonas spp. are important plant pathogens that seriously endanger crop yields and food security. RpfF is a key enzyme that is involved in the synthesis of diffusible signal factor (DSF) signals and predominates in the signaling pathway regulating quorum sensing (QS) in Xanthomonas. Currently, novel RpfF enzyme-based quorum sensing agents have been proposed as a promising strategy for the development of new pesticides. However, few reports are available that comprehensively summarize the progress in this field. Therefore, we provide a comprehensive review of the recent advances in DSF-mediated QS and recently reported inhibitors that are proposed as bactericide candidates to target the RpfF enzyme and control plant bacterial diseases.

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Section: Dsf Biosynthasementioning

confidence: 99%

“…In 2010, Cheng et al obtained the crystal structure of the RpfF protein through co-expression of both the RpfF and REC domains of RpfC in E. coli [ 51 ]. As illustrated in Figure 4 , the RpfF with an N-terminal α / β spiral core domain and a C-terminal α -helical region belongs to the enoyl-CoA hydratase/isomerase family.…”

Section: Dsf Biosynthasementioning

confidence: 99%

Research on Diffusible Signal Factor-Mediated Quorum Sensing in Xanthomonas: A Mini-Review

et al. 2023

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“…4B). The mechanism for UFA biosynthesis in X. campestris remains elusive, and it has been suggested that UFAs may be generated through a novel enzyme or pathway [39].…”

Section: Xc_plsc Protein Levels Respond To Environmental Conditionsmentioning

confidence: 99%

Characterization of multiple lysophosphatidic acid acyltransferases in the plant pathogen Xanthomonas campestris

Vasilopoulos,

Heflik,

Czolkoss

et al. 2023

The FEBS Journal

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Phosphatidic acid (PA) is the precursor of most phospholipids like phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin. In bacteria, its biosynthesis begins with the acylation of glycerol‐3‐phosphate to lysophosphatidic acid (LPA), which is further acylated to PA by the PlsC enzyme. Some bacteria, like the plant pathogen Xanthomonas campestris, use a similar pathway to acylate lysophosphatidylcholine to phosphatidylcholine (PC). Previous studies assigned two acyltransferases to PC formation. Here, we set out to study their activity and found a second much more prominent function of these enzymes in LPA to PA conversion. This PlsC‐like activity was supported by the functional complementation of a temperature‐sensitive plsC‐deficient Escherichia coli strain. Biocomputational analysis revealed two further PlsC homologs in X. campestris. The cellular levels of the four PlsC‐like proteins varied with respect to growth phase and growth temperature. To address the question whether these enzymes have redundant or specific functions, we purified two recombinant, detergent‐solubilized enzymes in their active form, which enabled the first direct biochemical comparison of PlsC isoenzymes from the same organism. Overlapping but not identical acyl acceptor and acyl donor preferences suggest redundant and specialized functions of the X. campestris PlsC enzymes. The altered fatty acid composition in plsC mutant strains further supports the functional differentiation of these enzymes.

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An atypical 3-ketoacyl ACP synthase III required for acyl homoserine lactone synthesis in Pseudomonas syringae pv. syringae B728a

Guo,

Su,

Liao

et al. 2024

Appl Environ Microbiol

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The last step of the initiation phase of fatty acid biosynthesis in most bacteria is catalyzed by the 3-ketoacyl-acyl carrier protein (ACP) synthase III (FabH). Pseudomonas syringae pv. syringae strain B728a encodes two FabH homologs, Psyr_3467 and Psyr_3830, which we designated PssFabH1 and PssFabH2, respectively. Here, we explored the roles of these two 3-ketoacyl-ACP synthase (KAS) III proteins. We found that PssFabH1 is similar to the Escherichia coli FabH in using acetyl-acetyl-coenzyme A (CoA ) as a substrate in vitro, whereas PssFabH2 uses acyl-CoAs (C 4 –C 10 ) or acyl-ACPs (C 6 –C 10 ). Mutant analysis showed that neither KAS III protein is essential for the de novo fatty acid synthesis and cell growth. Loss of PssFabH1 reduced the production of an acyl homoserine lactone (AHL) quorum-sensing signal, and this production was partially restored by overexpressing FabH homologs from other bacteria. AHL production was also restored by inhibiting fatty acid elongation and providing exogenous butyric acid. Deletion of PssFabH1 supports the redirection of acyl-ACP toward biosurfactant synthesis, which in turn enhances swarming motility. Our study revealed that PssFabH1 is an atypical KAS III protein that represents a new KAS III clade that functions in providing a critical fatty acid precursor, butyryl-ACP, for AHL synthesis. IMPORTANCE Acyl homoserine lactones (AHLs) are important quorum-sensing compounds in Gram-negative bacteria. Although their formation requires acylated acyl carrier proteins (ACPs), how the acylated intermediate is shunted from cellular fatty acid synthesis to AHL synthesis is not known. Here, we provide in vivo evidence that Pseudomonas syringae strain B728a uses the enzyme PssFabH1 to provide the critical fatty acid precursor butyryl-ACP for AHL synthesis. Loss of PssFabH1 reduces the diversion of butyryl-ACP to AHL, enabling the accumulation of acyl-ACP for synthesis of biosurfactants that contribute to bacterial swarming motility. We report that PssFabH1 and PssFabH2 each encode a 3-ketoacyl-acyl carrier protein synthase (KAS) III in P. syringae B728a. Whereas PssFabH2 is able to function in redirecting intermediates from β-oxidation to fatty acid synthesis, PssFabH1 is an atypical KAS III protein that represents a new KAS III clade based on its sequence, non-involvement in cell growth, and novel role in AHL synthesis.

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The FabA-FabB Pathway Is Not Essential for Unsaturated Fatty Acid Synthesis but Modulates Diffusible Signal Factor Synthesis in Xanthomonas campestris pv. campestris

Cited by 4 publications

References 56 publications

Research on Diffusible Signal Factor-Mediated Quorum Sensing in Xanthomonas: A Mini-Review

Research on Diffusible Signal Factor-Mediated Quorum Sensing in Xanthomonas: A Mini-Review

Characterization of multiple lysophosphatidic acid acyltransferases in the plant pathogen Xanthomonas campestris

An atypical 3-ketoacyl ACP synthase III required for acyl homoserine lactone synthesis in Pseudomonas syringae pv. syringae B728a

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