Faculty Opinions recommendation of A missense mutation in the fabB (beta-ketoacyl-acyl carrier protein synthase I) gene confers tiolactomycin resistance to Escherichia coli.

2002 ◽  
Author(s):  
Juan Luis Ramos
Keyword(s):  
Escherichia Coli ◽  
Missense Mutation ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
I Gene

Synthesis, cloning, and expression in Escherichia coli of a spinach acyl carrier protein-I gene

1987 ◽  
Vol 256 (1) ◽  
pp. 90-100 ◽  
Author(s):  
Phillip D. Beremand ◽  
David J. Hannapel ◽  
Daniel J. Guerra ◽  
David N. Kuhn ◽  
John B. Ohlrogge
Keyword(s):  
Escherichia Coli ◽  
Acyl Carrier Protein ◽  
Cloning And Expression ◽  
Carrier Protein ◽  
Expression In Escherichia Coli ◽  
I Gene

scholarly journals A Missense Mutation in the fabB (β-Ketoacyl-Acyl Carrier Protein Synthase I) Gene Confers Thiolactomycin Resistance to Escherichia coli

2002 ◽  
Vol 46 (5) ◽  
pp. 1246-1252 ◽  
Author(s):  
Suzanne Jackowski ◽  
Yong-Mei Zhang ◽  
Allen C. Price ◽  
Stephen W. White ◽  
Charles O. Rock
Keyword(s):  
Escherichia Coli ◽  
Missense Mutation ◽  
Acyl Carrier Protein ◽  
Side Chain ◽  
Binary Complex ◽  
Carrier Protein ◽  
Type I ◽  
Missense Mutations ◽  
Secretion Systems ◽  
Methyl Group

ABSTRACT Thiolactomycin (TLM) is an antibiotic that inhibits bacterial type II fatty acid synthesis at the condensing enzyme step, and β-ketoacyl-acyl carrier protein synthase I (FabB) is the relevant target in Escherichia coli. TLM resistance is associated with the upregulation of efflux pumps. Therefore, a tolC knockout mutant (strain ANS1) was constructed to eliminate the contribution of type I secretion systems to TLM resistance. Six independent TLM-resistant clones of strain ANS1 were isolated, and all possessed the same missense mutation in the fabB gene (T1168G) that directed the expression of a mutant protein, FabB(F390V). FabB(F390V) was resistant to TLM in vitro. Leucine is the only other amino acid found at position 390 in nature, and the Staphylococcus aureus FabF protein, which contains this substitution, was sensitive to TLM. Structural modeling predicted that the CG2 methyl group of the valine side chain interfered with the positioning of the C11 methyl on the isoprenoid side chain of TLM in the binary complex, whereas the absence of a bulky methyl group on the leucine side chain permitted TLM binding. These data illustrate that missense mutations that introduce valine at position 390 confer TLM resistance while maintaining the vital catalytic properties of FabB.

scholarly journals The Stability of Acyl Carrier Protein in Escherichia coli

1973 ◽  
Vol 248 (12) ◽  
pp. 4461-4466
Author(s):  
Gary L. Powell ◽  
Michael Bauza ◽  
Allan R. Larrabee
Keyword(s):  
Escherichia Coli ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
The Stability

scholarly journals Mutants of Escherichia coli with Temperature-sensitive Malonyl Coenzyme A-Acyl Carrier Protein Transacylase

1974 ◽  
Vol 249 (23) ◽  
pp. 7468-7475
Author(s):  
Mark E. Harder ◽  
Ruth C. Ladenson ◽  
Steven D. Schimmel ◽  
David F. Silbert
Keyword(s):  
Escherichia Coli ◽  
Coenzyme A ◽  
Acyl Carrier Protein ◽  
Temperature Sensitive ◽  
Carrier Protein

scholarly journals Steric Course of Reaction Catalyzed by the Enoyl Acyl-Carrier-Protein Reductase of Escherichia coli

1981 ◽  
Vol 116 (3) ◽  
pp. 581-586 ◽  
Author(s):  
Kazuki SAITO ◽  
Akihiko KAWAGUCHI ◽  
Yousuke SEYAMA ◽  
Tamio YAMAKAWA ◽  
Shigenobu OKUDA
Keyword(s):  
Escherichia Coli ◽  
Acyl Carrier Protein ◽  
Carrier Protein
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