Essential Fatty Acid Biosynthetic Enzymes of Escherichia Coli and Lactococcus Lactis Subsp. Lactis

FabG, beta-ketoacyl-ACP reductase, performs the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to the beta-hydroxyacyl-ACP products. I report the first characterized fabG mutants. By chemical mutagenesis followed by a tritium suicide procedure, I obtained three conditionally-lethal temperature-sensitive fabG (fabGts) mutants. The E. coli mutant has two point mutations: A154T and E233K. In Salmonella enterica Serovar Typhimurium fabGts mutants one strain had a point mutation, S224F whereas the second strain contained two mutations (M125I and A223T). All of the altered residues of the FabG mutant proteins are located on or near the two-fold axes of symmetry at the dimer interfaces in this homotetrameric protein suggesting that the quanternary structures of the mutant FabG proteins may be disrupted at the nonpermissive temperature.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Microbiology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Lai, Chiou-Yan

Contributors dc:contributor

• Cronan, John E., Jr

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI3101892

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/86655