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Table 1 Mutations that occurred in the strains isolated from the evolution experiment

From: Evolutionary engineering of E. coli MG1655 for tolerance against isoprenol

Gene Genomic coordinate Nucleotide change Effect of nucleotide change Frequency (%) Time Description
257,908 G → A   5 T5 IS1 non-coding
frmR (1) 379,625 A → C V(86) → G 5 T7 Formaldehyde repressor
frmR (2) 379,821 − 1:C Q(21) → frameshift 5 T7
gltA 754,123 C → T E(116) → K 10 T4 Citrate synthase
plsX (1) 1,148,440 − 1:A Q(274)KS → QRA STOP 10 T3 Fatty acid/phospholipid synthesis protein
plsX (2) 1,148,491 G → T G(291) → C 10 T4
fabF (1) 1,152,159 T → G F(74) → C 48 T3 Component of 3-oxoacyl-ACP synthase II
fabF (2) 1,152,159 C → T wt 5 T4
marC (1) 1,618,245 A → T stop → frameshift 10 T4 Inner membrane protein
marC (2) 1,618,498 − 7:ATCGCTA I(135) → stop 10 T2
marC (3) 1,618,805 − 1:T M(35) → stop 48 T3
yffS 2,564,930 G → T A → A (silent) 5 T3 CPZ-55 prophage; uncharacterized protein
yfgO 2,615,421 G → A A(154) → V 5 T2 Function unknown, predicted membrane permease
iscR 2,661,812 T → A H(107) → L 10 T5 Iron–sulfur cluster regulator
srmB 2,713,364 G → A D(157) → N 10 T2 SrmB is a DEAD-box protein with RNA helicase activity that facilitates an early step in the assembly of the 50S subunit of the ribosome
PyghB 3,153,480 − 15   33 T4 Required, with yqjA, for membrane integrity
trkH 4,033,611 G → A G(156) → D 10 T5 TrkH is a potassium ion transporter
rraA (1) 4,119,044 A → T V(96) → E 10 T4 RraA inhibits ribonuclease E activity by binding to and masking the C-terminal RNA binding domain of RNase E
rraA (2) 4,119,138 C → T G(67) → S 5 T4
plsB 4,255,502 T → C Q(322) → R 5 T2 Membrane-bound glycerol-3-phosphate acyltransferase catalyzes the first committed step in phospholipid biosynthesis
Rob (1) 4,634,494 C → A G(273) → stop 5 T5 Transcriptional regulator implied in solvent tolerance
Rob (2) 4,635,002  + 1:T Y(103) → stop 10 T6
Rob (3) 4,635,168  + 1:G H(48) → frameshift 19 T6
creC 4,637,267 T → G L (191) → W 5 T5 Carbon source responsive sensor kinase
  1. Protein functions are taken from ecocyc.org. For genes with alternative mutations, the numbering behind the gene name refers to the mutation name provided in Fig. 2