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Abstract GDP-l-galactose phosphorylase (GGP) is a key rate-limiting enzyme in plant ascorbic acid synthesis, which plays an important role in plant growth and development as well as stress response. However, the presence of GGP and its function in potato and pepper are not known. In this study, we first identified two GGP genes in each potato and pepper genomes using a genome-wide search approach. We then analyzed their physicochemical properties, conserved domains, protein structures and phylogenetic relationships. Phylogenetic tree analysis revealed that members of the potato and pepper GGP gene families are related to eggplant (Solanum melongena L.), Arabidopsis (Arabidopsis thaliana L.), tobacco (Nicotiana tabacum L.) and tomato (Solanum lycopersicum L.), with tomato being the most closely related. The promoter sequences mainly contain homeopathic elements such as light-responsive, hormone-responsive and stress-responsive, with light-responsive elements being the most abundant. By analyzing the structure of the genes, it was found that there is no transmembrane structure or signal peptide in the GGP gene family of potatoes and peppers, and that all of its members are hydrophilic proteins. The expression profiles of different tissues show that StGGP1 has the highest expression levels in leaves, StGGP2 has the highest expression levels in stamens, and CaGGPs have the highest expression levels in the early stages of fruit development (Dev1). It was found that StGGPs and CaGGPs genes showed different response to phytohormones and abiotic stresses. Abscisic acid (ABA) treatment induced the most significant change in the expression of StGGPs, while the expression of CaGGPs showed the most pronounced change under methyl jasmonate (MeJA) treatment. StGGPs responded mainly to dark treatment, whereas CaGGPs responded mainly to NaCl stress. These results provide an important basis for a detailed study about the functions of GGP homologous genes in potato and pepper in response to abiotic stresses.

Abstract The 3-ketoacyl-ACP synthase III (FabH), a key enzyme for bacteria growth, catalyses the last step of the initiation of bacterial fatty acid synthesis. Rice bacterial blight is caused by the pathogen Xanthomonas oryzae pv. oryzae (Xoo), which is widely studied as a model bacterium. Bioinformatics analysis showed that the X. oryzae pv. oryzae PXO99A genome encodes three FabH homologous proteins with unknown functions. In this study, we found that only PXO_02706 (fabH1) encodes a functional FabH, the key enzyme in the production of branched-chain fatty acid, which is essential for the branched-chain diffusible signal factor family signals in Xoo. Interestingly, we found that FabH1 is not essential for fatty acid biosynthesis in Xoo. Pathogenicity analysis showed that loss of fabH1 caused a significant decrease in virulence of Xoo. Genetic and phenotypic analyses revealed that fabH1 plays a key role in multiple Xoo virulence-related activities, including exopolysaccharide (EPS) production, biofilm formation, motility, and resistance to environmental stresses.

The adverse impact of macroalgal blooms associated with nutrient enrichment on seagrass habitats and carbon storage potential is an ecological concern. In the present study, the soil carbon stock and sources were compared between a seagrass meadow where a serious macroalgal bloom occurred (site M) and an adjacent site without apparent macroalgae (site R) in a nutrient-enriched lagoon in South Hainan Island, China, to test whether macroalgal blooms associated with nutrient enrichment would impact the soil carbon in seagrass meadows. The soil organic carbon (OC) and total nitrogen contents in the top 30 cm at site M were significantly lower than those at site R. The soil OC stocks (top 30 cm) were 3.4 and 5.4 Mg C ha-1 at site M and site R, respectively, and no difference was observed between sampling stations with different distances offshore at either site. Soil δ13C was more enriched and closer to the δ13C of seagrass tissues at site R than at site M. Bayesian stable isotope mixing model analyses suggested that seagrass-derived material contributed ~50% to soil OC at site R, while at site M, the contribution was reduced to ~25%. The results suggested that macroalgal blooms associated with nutrient enrichment could drive the loss of seagrass-derived OC and the OC stock in the soil, which is worthy of full attention for blue carbon conservation.

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 (C4–C10) or acyl-ACPs (C6–C10). 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. [ABSTRACT FROM AUTHOR]