Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Biosynthesis of the red antibiotic, prodigiosin, in Serratia : identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces. / Williamson, Neil R; Simonsen, Henrik Toft; Ahmed, Raef A A; Goldet, Gabrielle; Slater, Holly; Woodley, Louise; Leeper, Finian J; Salmond, George P C.

In: Molecular Microbiology, Vol. 56, No. 4, 05.2005, p. 971-89.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Williamson, NR, Simonsen, HT, Ahmed, RAA, Goldet, G, Slater, H, Woodley, L, Leeper, FJ & Salmond, GPC 2005, 'Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces', Molecular Microbiology, vol. 56, no. 4, pp. 971-89. https://doi.org/10.1111/j.1365-2958.2005.04602.x

APA

Williamson, N. R., Simonsen, H. T., Ahmed, R. A. A., Goldet, G., Slater, H., Woodley, L., Leeper, F. J., & Salmond, G. P. C. (2005). Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces. Molecular Microbiology, 56(4), 971-89. https://doi.org/10.1111/j.1365-2958.2005.04602.x

Vancouver

Williamson NR, Simonsen HT, Ahmed RAA, Goldet G, Slater H, Woodley L et al. Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces. Molecular Microbiology. 2005 May;56(4):971-89. https://doi.org/10.1111/j.1365-2958.2005.04602.x

Author

Williamson, Neil R ; Simonsen, Henrik Toft ; Ahmed, Raef A A ; Goldet, Gabrielle ; Slater, Holly ; Woodley, Louise ; Leeper, Finian J ; Salmond, George P C. / Biosynthesis of the red antibiotic, prodigiosin, in Serratia : identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces. In: Molecular Microbiology. 2005 ; Vol. 56, No. 4. pp. 971-89.

Bibtex

@article{af35519547b74b7890ee7aca1a9a1ebb,
title = "Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces",
abstract = "The biosynthetic pathway of the red-pigmented antibiotic, prodigiosin, produced by Serratia sp. is known to involve separate pathways for the production of the monopyrrole, 2-methyl-3-n-amyl-pyrrole (MAP) and the bipyrrole, 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC) which are then coupled in the final condensation step. We have previously reported the cloning, sequencing and heterologous expression of the pig cluster responsible for prodigiosin biosynthesis in two Serratia sp. In this article we report the creation of in-frame deletions or insertions in every biosynthetic gene in the cluster from Serratia sp. ATCC 39006. The biosynthetic intermediates accumulating in each mutant have been analysed by LC-MS, cross-feeding and genetic complementation studies. Based on these results we assign specific roles in the biosynthesis of MBC to the following Pig proteins: PigI, PigG, PigA, PigJ, PigH, PigM, PigF and PigN. We report a novel pathway for the biosynthesis of MAP, involving PigD, PigE and PigB. We also report a new chemical synthesis of MAP and one of its precursors, 3-acetyloctanal. Finally, we identify the condensing enzyme as PigC. We reassess the existing literature and discuss the significance of the results for the biosynthesis of undecylprodigiosin by the Red cluster in Streptomyces coelicolor A3(2).",
keywords = "Anti-Bacterial Agents, Molecular Structure, Multigene Family, Mutation, Prodigiosin, Pyrroles, Serratia, Streptomyces coelicolor",
author = "Williamson, {Neil R} and Simonsen, {Henrik Toft} and Ahmed, {Raef A A} and Gabrielle Goldet and Holly Slater and Louise Woodley and Leeper, {Finian J} and Salmond, {George P C}",
year = "2005",
month = may,
doi = "10.1111/j.1365-2958.2005.04602.x",
language = "English",
volume = "56",
pages = "971--89",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley-Blackwell",
number = "4",

}

RIS

TY - JOUR

T1 - Biosynthesis of the red antibiotic, prodigiosin, in Serratia

T2 - identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces

AU - Williamson, Neil R

AU - Simonsen, Henrik Toft

AU - Ahmed, Raef A A

AU - Goldet, Gabrielle

AU - Slater, Holly

AU - Woodley, Louise

AU - Leeper, Finian J

AU - Salmond, George P C

PY - 2005/5

Y1 - 2005/5

N2 - The biosynthetic pathway of the red-pigmented antibiotic, prodigiosin, produced by Serratia sp. is known to involve separate pathways for the production of the monopyrrole, 2-methyl-3-n-amyl-pyrrole (MAP) and the bipyrrole, 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC) which are then coupled in the final condensation step. We have previously reported the cloning, sequencing and heterologous expression of the pig cluster responsible for prodigiosin biosynthesis in two Serratia sp. In this article we report the creation of in-frame deletions or insertions in every biosynthetic gene in the cluster from Serratia sp. ATCC 39006. The biosynthetic intermediates accumulating in each mutant have been analysed by LC-MS, cross-feeding and genetic complementation studies. Based on these results we assign specific roles in the biosynthesis of MBC to the following Pig proteins: PigI, PigG, PigA, PigJ, PigH, PigM, PigF and PigN. We report a novel pathway for the biosynthesis of MAP, involving PigD, PigE and PigB. We also report a new chemical synthesis of MAP and one of its precursors, 3-acetyloctanal. Finally, we identify the condensing enzyme as PigC. We reassess the existing literature and discuss the significance of the results for the biosynthesis of undecylprodigiosin by the Red cluster in Streptomyces coelicolor A3(2).

AB - The biosynthetic pathway of the red-pigmented antibiotic, prodigiosin, produced by Serratia sp. is known to involve separate pathways for the production of the monopyrrole, 2-methyl-3-n-amyl-pyrrole (MAP) and the bipyrrole, 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC) which are then coupled in the final condensation step. We have previously reported the cloning, sequencing and heterologous expression of the pig cluster responsible for prodigiosin biosynthesis in two Serratia sp. In this article we report the creation of in-frame deletions or insertions in every biosynthetic gene in the cluster from Serratia sp. ATCC 39006. The biosynthetic intermediates accumulating in each mutant have been analysed by LC-MS, cross-feeding and genetic complementation studies. Based on these results we assign specific roles in the biosynthesis of MBC to the following Pig proteins: PigI, PigG, PigA, PigJ, PigH, PigM, PigF and PigN. We report a novel pathway for the biosynthesis of MAP, involving PigD, PigE and PigB. We also report a new chemical synthesis of MAP and one of its precursors, 3-acetyloctanal. Finally, we identify the condensing enzyme as PigC. We reassess the existing literature and discuss the significance of the results for the biosynthesis of undecylprodigiosin by the Red cluster in Streptomyces coelicolor A3(2).

KW - Anti-Bacterial Agents

KW - Molecular Structure

KW - Multigene Family

KW - Mutation

KW - Prodigiosin

KW - Pyrroles

KW - Serratia

KW - Streptomyces coelicolor

U2 - 10.1111/j.1365-2958.2005.04602.x

DO - 10.1111/j.1365-2958.2005.04602.x

M3 - Journal article

C2 - 15853884

VL - 56

SP - 971

EP - 989

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 4

ER -

ID: 128571062