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|Title:||Characterization and analysis of genes encoding Escherichia coli acetyl-CoA carboxylase|
|Doctoral Committee Chair(s):||Cronan, John E.|
|Department / Program:||Microbiology|
|Degree Granting Institution:||University of Illinois at Urbana-Champaign|
|Abstract:||Acetyl-CoA carboxylase catalyzes the first committed step of fatty acid biosynthesis, the synthesis of malonyl-CoA. In Escherichia coli the enzyme is a complex of four subunits that catalyzes two distinct half-reactions.
I have cloned and determined the nucleotide sequences of the genes encoding biotin carboxylase, BCCP (map at min 72), and carboxyltransferase subunits (The $\alpha$ subunit map at min 4.3 and the $\beta$ subunit map at min 50). I have also defined the sequence requirement for biotination of the BCCP subunit by protein fusion analyses. Peptide mapping of the purified carboxyltransferase indicates that this enzyme component is a complex of two nonidentical subunits. In addition, I have identified putative functional domains within the deduced amino acid sequences. The identified domains include sequences that involves in ATP, bicarbonate binding (biotin carboxylase), in biotination (BCCP), and in CoA binding (carboxyltransferase).
To investigate the regulation of acetyl-CoA carboxylase genes, I monitored the transcription levels of these genes under a variety of growth conditions. A direct correlation was found between the levels of acc genes transcripts and the rate of cellular growth.
|Rights Information:||Copyright 1992 Li, Shyr-Jiann|
|Date Available in IDEALS:||2011-05-07|
|Identifier in Online Catalog:||AAI9305602|