Essential Fatty Acid Biosynthetic Enzymes of Escherichia Coli and Lactococcus Lactis Subsp. Lactis
Lai, Chiou-Yan
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https://hdl.handle.net/2142/86655
Description
Title
Essential Fatty Acid Biosynthetic Enzymes of Escherichia Coli and Lactococcus Lactis Subsp. Lactis
Author(s)
Lai, Chiou-Yan
Issue Date
2003
Doctoral Committee Chair(s)
Cronan, John E., Jr
Department of Study
Microbiology
Discipline
Microbiology
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
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.
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