<b>The Structure of Serratamolide<sup>1-3</sup></b>

Wasserman, Harry H.; Keggi, Janis J.; McKeon, James E.

doi:10.1021/ja00874a028

Cited by 72 publications

(39 citation statements)

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“…serratamolide reported previously as an antibiotic (22,23). It is interesting that production of these serrawettins is also temperature-dependent (10).…”

mentioning

confidence: 76%

Identification and Characterization of the pswP Gene Required for the Parallel Production of Prodigiosin and Serrawettin W1 in Serratia marcescens

Sunaga

Sato

et al. 2004

Microbiology and Immunology

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Serratia marcescens mutants defective in production of the red pigment prodigiosin and the biosurfactant serrawettin W1 in parallel were isolated by transposon mutagenesis of strain 274. Cloning of the DNA fragment required for production of these secondary metabolites with different chemical structures pointed out a novel open reading frame (ORF) named pswP. The putative product PswP (230 aa) has the distinct signature sequence consensus among members of phosphopantetheinyl transferase (PPTase) which phosphopantetheinylates peptidyl carrier protein (PCP) mostly integrated in the nonribosomal peptide synthetases (NRPSs) system. Since serrawettin W1 belongs to the cyclodepsipeptides, which are biosynthesized through the NRPSs system, and one pyrrole ring in prodigiosin has been reported as a derivative of L‐proline tethered to phosphopantetheinylated PCP, the mutation in the single gene pswP seems responsible for parallel failure in production of prodigiosin and serrawettin W1.

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“…serratamolide reported previously as an antibiotic (22,23). It is interesting that production of these serrawettins is also temperature-dependent (10).…”

mentioning

confidence: 76%

Identification and Characterization of the pswP Gene Required for the Parallel Production of Prodigiosin and Serrawettin W1 in Serratia marcescens

Sunaga

Sato

et al. 2004

Microbiology and Immunology

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“…A distinct group of the Dps mutants (DpsI) appeared not to produce the extracellular slime layer generally visible around the bacterial colony. We show here that some of the DpsI mutants as well as some Dis (completely defective in swarming) mutants are defective in the production of serrawettin W1, an extracellular cyclic lipopeptide (14,24). Flagellum-independent spreading of S. marcescens 274 on the surface of low-agar media also requires serrawettin.…”

mentioning

confidence: 78%

“…Serrawettin W1, produced by many pigmented S. marcescens strains, is a surface-active cyclodepsipeptide [cyclo-(D-3-hydroxydecanoyl-L-seryl) 2 ] identical to serratamolide, which was discovered by Wasserman et al as an antibiotic (23,24). Serrawettin gets its name by virtue of its wetting activity on various hydrophobic and hydrophilic surfaces (14).…”

Section: Discussionmentioning

confidence: 99%

Mutational analysis of flagellum-independent surface spreading of Serratia marcescens 274 on a low-agar medium

1995

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In a previous study (J. O'Rear, L. Alberti, and R. M. Harshey, J. Bacteriol. 174:6125-6137, 1992) we reported the isolation of several transposon mutants of Serratia marcescens 274 that were defective either in swarming alone or in both swimming and swarming motility. All the nonflagellate (Fla ؊ ) mutants, while defective in both types of motility, were able to spread rapidly on the surface of low-agar (0.35%) media. We show here that some of the swarming-defective mutants are defective in the production of serrawettin W1, an extracellular cyclic lipopeptide produced by S. marcescens 274. When combined with a Fla defect, the serrawettin (Swt) mutants are deficient in spreading on low-agar media. The spreading deficiency can be overcome by serrawettin supplied extracellularly. Introduction of Fla defects into chemotaxis mutants does not affect this mode of surface translocation. These results suggest that spreading may be a passive form of translocation. We also report that swarming defects in all mutants showing a Dps phenotype (able to swarm within the inoculated area but unable to move outward) in the earlier study can be overcome by changing the commercial source of agar.Serratia marcescens is a pigmented enteric bacterium found in variety of niches, which include soil, water, air, plants, and animals (9). It is also an opportunistic human pathogen, causing many nosocomial infections (7). S. marcescens is unique among enteric bacteria in many respects. It secretes extracellular chitinases, several proteases, a nuclease, and a lipase (13) and produces a wetting agent or surfactant called serrawettin, which helps in the colonization of surfaces (14,15,17). In keeping with its varied habitat, S. marcescens produces alternate forms of differentially flagellated cells which display different types of motility depending on whether the growth medium is liquid or solid (2). Nonflagellated cells of S. marcescens can also translocate (spread) efficiently over the surface of low-agar media (20).Surface colonization via swarming requires the flagellar apparatus as well the chemotaxis system (20). A large-scale transposon mutagenesis study of S. marcescens identified several additional functions that were needed for swarming (20). A sizable subset of the mutants showed a Dps phenotype (cells were capable of swarming but remained confined to the inoculated area, i.e., were unable to move outwards). A distinct group of the Dps mutants (DpsI) appeared not to produce the extracellular slime layer generally visible around the bacterial colony. We show here that some of the DpsI mutants as well as some Dis (completely defective in swarming) mutants are defective in the production of serrawettin W1, an extracellular cyclic lipopeptide (14, 24). Flagellum-independent spreading of S. marcescens 274 on the surface of low-agar media also requires serrawettin. Defects in chemotaxis functions, however, had no effect on this mode of surface colonization. Our results reveal the importance of bacterial surface layers (serrawettins, slim...

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“…Some β-hydroxy fatty acids (e.g. β-hydroxydodecanoic acid), are constituents of peptide antibiotics such as esperin [42], serratamolide [43], and isariin [44]. Long-chain α-hydroxy-fatty acids are constituents of brain lipids, and of sphingolipids, which are essential components of cell membranes.…”

Section: Physiological Roles and Chemical Applications Of Hydroxy Fatmentioning

confidence: 99%

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

2017

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The Structure of Serratamolide^1-3

Cited by 72 publications

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Identification and Characterization of the pswP Gene Required for the Parallel Production of Prodigiosin and Serrawettin W1 in Serratia marcescens

Identification and Characterization of the pswP Gene Required for the Parallel Production of Prodigiosin and Serrawettin W1 in Serratia marcescens

Mutational analysis of flagellum-independent surface spreading of Serratia marcescens 274 on a low-agar medium

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

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The Structure of Serratamolide1-3

Cited by 72 publications

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Identification and Characterization of the pswP Gene Required for the Parallel Production of Prodigiosin and Serrawettin W1 in Serratia marcescens

Identification and Characterization of the pswP Gene Required for the Parallel Production of Prodigiosin and Serrawettin W1 in Serratia marcescens

Mutational analysis of flagellum-independent surface spreading of Serratia marcescens 274 on a low-agar medium

Regioselective Biocatalytic Hydroxylation of Fatty Acids by Cytochrome P450s

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The Structure of Serratamolide^1-3