Additional file 1 of Speed dating for enzymes! Finding the perfect phosphopantetheinyl transferase partner for your polyketide synthase
journal contributionposted on 2022-01-11, 04:40 authored by Tobias Bruun Pedersen, Mikkel Rank Nielsen, Sebastian Birkedal Kristensen, Eva Mie Lang Spedtsberg, Trine Sørensen, Celine Petersen, Jens Muff, Teis Esben Sondergaard, Kåre Lehmann Nielsen, Reinhard Wimmer, Donald Max Gardiner, Jens Laurids Sørensen
Additional file 1: Table S1. This table contains the primer sequences of both the primers used for gene-amplification and the primer used for initial sanger-sequencing in fragments of around 700 bp, containing at least 50 bp overlap between each fragment. Table S2. This table contains the different plasmids utilized in the project, both the native plasmids used as expression vectors, but also plasmids purchased containing the synthetically derived codon optimized genes. Figure S1. Phylogenetic tree of the PPTases used in the present study (bold) together with 22 additional published PPTases. Bootstrap values (> 70%) from 1000 replications are indicated at the respective nodes. Figure S2. Predicted structure of sfp/ACP interaction with the CoA and Mg2+ ion highlighted by arrows. Figure S3. Production levels of bikaverin and bostrycoidin in the individual strains (relative to OD at 48 h) in the supernatant and pellets. The mean of the supernatant from BY4743::FvPPT1 was set to 100 for both compounds.
Teknologi og Produktion, Det Frie Forskningsråd Novo Nordisk Fonden
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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