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Massetolide A biosynthesis in Pseudomonas fluorescens.

I de Bruijn¹, M J D de Kock, P de Waard

¹Laboratory of Phytopathology, Wageningen University, The Netherlands.

Journal of Bacteriology

|November 13, 2007

Summary

Massetolide A biosynthesis in Pseudomonas fluorescens SS101 involves three nonribosomal peptide synthetase (NRPS) genes (massA, massB, massC). This cyclic lipopeptide antibiotic is crucial for swarming motility and biofilm formation.

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Area of Science:

Microbiology
Molecular Biology
Biochemistry

Background:

Massetolide A is a cyclic lipopeptide (CLP) antibiotic produced by Pseudomonas strains.
Understanding the genetic basis of CLP biosynthesis is crucial for antibiotic discovery and development.
Previous studies have identified various CLP biosynthesis gene clusters in Pseudomonas species.

Purpose of the Study:

To elucidate the genetic organization and regulation of massetolide A biosynthesis in Pseudomonas fluorescens SS101.
To investigate the role of massetolide A in bacterial physiology, including motility and biofilm formation.
To analyze the structural variations within the massetolide A peptide moiety.

Main Methods:

Cloning, sequencing, and site-directed mutagenesis of nonribosomal peptide synthetase (NRPS) genes (massA, massB, massC).
In silico analysis of NRPS adenylation and condensation domains for amino acid prediction.
Quantitative real-time PCR (qRT-PCR) to analyze gene transcription.
Structural analysis of massetolide A derivatives.
Assessment of swarming motility and biofilm formation in P. fluorescens SS101.

Main Results:

Massetolide A biosynthesis is governed by three NRPS genes (massA, massB, massC) organized into two separate clusters.
MassB and massC appear to function as an operon, while massA transcription is independent.
Structural analysis revealed variations in amino acid positions 4 and 9 of the peptide moiety.
Massetolide A production is essential for swarming motility and plays a significant role in biofilm formation.
Biosynthesis occurs during the early exponential growth phase and is not regulated by N-acylhomoserine lactone-based quorum sensing.

Conclusions:

The genetic organization of massetolide A biosynthesis differs from previously characterized Pseudomonas CLP gene clusters.
Massetolide A is a key factor in the ecological fitness of P. fluorescens SS101, influencing motility and biofilm development.
The findings provide insights into the complex regulation of CLP production in bacteria.