Speed dating for enzymes! Finding the perfect phosphopantetheinyl transferase partner for your polyketide synthase
Posted on 2022-01-11 - 04:40
Abstract The biosynthetic pathways for the fungal polyketides bikaverin and bostrycoidin, from Fusarium verticillioides and Fusarium solani respectively, were reconstructed and heterologously expressed in S. cerevisiae alongside seven different phosphopantetheinyl transferases (PPTases) from a variety of origins spanning bacterial, yeast and fungal origins. In order to gauge the efficiency of the interaction between the ACP-domains of the polyketide synthases (PKS) and PPTases, each were co-expressed individually and the resulting production of target polyketides were determined after 48 h of growth. In co-expression with both biosynthetic pathways, the PPTase from Fusarium verticillioides (FvPPT1) proved most efficient at producing both bikaverin and bostrycoidin, at 1.4 mg/L and 5.9 mg/L respectively. Furthermore, the remaining PPTases showed the ability to interact with both PKS’s, except for a single PKS-PPTase combination. The results indicate that it is possible to boost the production of a target polyketide, simply by utilizing a more optimal PPTase partner, instead of the commonly used PPTases; NpgA, Gsp and Sfp, from Aspergillus nidulans, Brevibacillus brevis and Bacillus subtilis respectively.
CITE THIS COLLECTION
DataCite
3 Biotech
3D Printing in Medicine
3D Research
3D-Printed Materials and Systems
4OR
AAPG Bulletin
AAPS Open
AAPS PharmSciTech
Abhandlungen aus dem Mathematischen Seminar der Universität Hamburg
ABI Technik (German)
Academic Medicine
Academic Pediatrics
Academic Psychiatry
Academic Questions
Academy of Management Discoveries
Academy of Management Journal
Academy of Management Learning and Education
Academy of Management Perspectives
Academy of Management Proceedings
Academy of Management Review
Pedersen, Tobias Bruun; Nielsen, Mikkel Rank; Kristensen, Sebastian Birkedal; Spedtsberg, Eva Mie Lang; Sørensen, Trine; Petersen, Celine; et al. (2022). Speed dating for enzymes! Finding the perfect phosphopantetheinyl transferase partner for your polyketide synthase. figshare. Collection. https://doi.org/10.6084/m9.figshare.c.5786722.v1
or
Select your citation style and then place your mouse over the citation text to select it.
SHARE
Usage metrics
Read the peer-reviewed publication
AUTHORS (12)
TP
Tobias Bruun Pedersen
MN
Mikkel Rank Nielsen
SK
Sebastian Birkedal Kristensen
ES
Eva Mie Lang Spedtsberg
TS
Trine Sørensen
CP
Celine Petersen
JM
Jens Muff
TS
Teis Esben Sondergaard
KN
Kåre Lehmann Nielsen
RW
Reinhard Wimmer
DG
Donald Max Gardiner
JS
Jens Laurids Sørensen
CATEGORIES
KEYWORDS
bacillus subtilis respectivelyorigins spanning bacterialremaining pptases showedpolyketide synthase abstractcommonly used pptasesfusarium solani respectivelyoptimal pptase partnerfungal polyketides bikaverinfungal originstarget polyketidesfusarium verticillioidestarget polyketidepolyketide synthasesl respectivelyspeed datingresults indicatepptase combinationheterologously expressedexpressed individuallybrevibacillus brevisbiosynthetic pathwaysaspergillus nidulans9 mg48 h4 mg