Alteration of Acyl-Acyl Carrier Protein Pools and Acetyl-CoA Carboxylase Expression in Escherichia coli by a Plant Medium-Chain Acyl-Acyl Carrier Protein Thioesterase

Alteration of Acyl-Acyl Carrier Protein Pools and Acetyl-CoA Carboxylase Expression in... Expression of a plant lauroyl-acyl carrier protein (ACP) thioesterase in an Escherichia coli strain deficient in beta oxidation results in the accumulation of free fatty acids in the culture. Overall fatty acid production by the cultures is increased severalfold, particularly in the late log and stationary stages of growth. In control E. coli cells, malonyl-ACP levels and rates of fatty acid synthesis are highest during rapid logarithmic growth and decline to undetectable levels in stationary stage. In contrast, in cells expressing plant acyl-ACP thioesterase, malonyl-ACP levels remain high in late log and stationary stage in association with the continued fatty acid production. In addition, the biotin carboxyl carrier protein component of acetyl-CoA carboxylase is expressed at higher levels in cultures expressing the acyl-ACP thioesterase. The data presented indicate that removal of the acyl-ACP products of fatty acid synthesis results in increased production of both malonyl-ACP and fatty acids, which may in turn result from higher activity and/or expression of acetyl-CoA carboxylase. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Biochemistry and Biophysics Elsevier

Alteration of Acyl-Acyl Carrier Protein Pools and Acetyl-CoA Carboxylase Expression in Escherichia coli by a Plant Medium-Chain Acyl-Acyl Carrier Protein Thioesterase

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Publisher
Elsevier
Copyright
Copyright © 1995 Academic Press
ISSN
0003-9861
eISSN
1096-0384
D.O.I.
10.1006/abbi.1995.1152
Publisher site
See Article on Publisher Site

Abstract

Expression of a plant lauroyl-acyl carrier protein (ACP) thioesterase in an Escherichia coli strain deficient in beta oxidation results in the accumulation of free fatty acids in the culture. Overall fatty acid production by the cultures is increased severalfold, particularly in the late log and stationary stages of growth. In control E. coli cells, malonyl-ACP levels and rates of fatty acid synthesis are highest during rapid logarithmic growth and decline to undetectable levels in stationary stage. In contrast, in cells expressing plant acyl-ACP thioesterase, malonyl-ACP levels remain high in late log and stationary stage in association with the continued fatty acid production. In addition, the biotin carboxyl carrier protein component of acetyl-CoA carboxylase is expressed at higher levels in cultures expressing the acyl-ACP thioesterase. The data presented indicate that removal of the acyl-ACP products of fatty acid synthesis results in increased production of both malonyl-ACP and fatty acids, which may in turn result from higher activity and/or expression of acetyl-CoA carboxylase.

Journal

Archives of Biochemistry and BiophysicsElsevier

Published: Feb 20, 1995

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