Investigations into the biosynthesis, regulation and self-resistance of toxoflavin in Pseudomonas protegens Pf-5.

TY - JOUR

T1 - Investigations into the biosynthesis, regulation and self-resistance of toxoflavin in Pseudomonas protegens Pf-5.

AU - Philmus, Benjamin

AU - Shaffer, Brenda

AU - Kidarsa, Teresa

AU - Yan, Qing

AU - Raaijmakers, Jos

AU - Begley, Tadhg

AU - Loper, Joyce

N1 - 5884, ME; Data archiving: Property of and archived at USDA

PY - 2015

Y1 - 2015

N2 - Pseudomonas spp. are prolific producers of natural products from many structural classes. Here we show that the soil bacterium Pseudomonas protegens Pf-5 is capable of producing trace levels of the triazine natural product toxoflavin (1) under microaerobic conditions. We evaluated toxoflavin production by derivatives of Pf-5 having deletions in specific biosynthesis genes, which led us to propose a new biosynthetic pathway for toxoflavin that shares the first two steps with riboflavin biosynthesis. We also report that toxM, which is not present in the well-characterized cluster of Burkholderia glumae, encodes a monooxygenase that degrades toxoflavin. The toxoflavin degradation product of ToxM is identical to that of TflA, the toxoflavin lyase from Paenibacillus polymyxa. Toxoflavin production by P. protegens causes inhibition of several plant-pathogenic bacteria, and introduction of toxM into the toxoflavin-sensitive strain P. syringae DC3000 results in resistance to toxoflavin.

AB - Pseudomonas spp. are prolific producers of natural products from many structural classes. Here we show that the soil bacterium Pseudomonas protegens Pf-5 is capable of producing trace levels of the triazine natural product toxoflavin (1) under microaerobic conditions. We evaluated toxoflavin production by derivatives of Pf-5 having deletions in specific biosynthesis genes, which led us to propose a new biosynthetic pathway for toxoflavin that shares the first two steps with riboflavin biosynthesis. We also report that toxM, which is not present in the well-characterized cluster of Burkholderia glumae, encodes a monooxygenase that degrades toxoflavin. The toxoflavin degradation product of ToxM is identical to that of TflA, the toxoflavin lyase from Paenibacillus polymyxa. Toxoflavin production by P. protegens causes inhibition of several plant-pathogenic bacteria, and introduction of toxM into the toxoflavin-sensitive strain P. syringae DC3000 results in resistance to toxoflavin.

KW - triazine

KW - secondary metabolism

KW - biocontrol

KW - international

U2 - 10.1002/cbic.201500247

DO - 10.1002/cbic.201500247

M3 - Article

SN - 1439-7633

VL - 16

SP - 1782

EP - 1790

JO - ChemBioChem

JF - ChemBioChem

IS - 12

ER -