In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis.

In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis. Research Abstract Details 

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In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis. Abstract Text:

Nicholas R De Lay,John E Cronan,

Acyl carrier protein (ACP) is a key component of the fatty acid synthesis pathways of both type I and type II synthesis systems. A large number of structure-function studies of various type II ACPs have been reported, but all are in vitro studies that assayed function or interaction of mutant ACPs with various enzymes of fatty acid synthesis or transfer. Hence in these studies functional properties of various mutant ACPs were assayed with only a subset of the many ACP-interacting proteins, which may not give an accurate overall view of the function of these proteins in vivo. This is especially so because Escherichia coli ACP has been reported to interact with several proteins that have no known roles in lipid metabolism. We therefore tested a large number of mutant derivatives of E. coli ACP carrying single amino acid substitutions for their abilities to restore growth to an E. coli strain carrying a temperature-sensitive mutation in acpP, the gene that encodes ACP. Many of these mutant proteins had previously been tested in vitro thus providing data for comparison with our results. We found that several mutant ACPs containing substitutions of ACP residues reported previously to be required for ACP function in vitro support normal growth of the acpP mutant strain. However, several mutant proteins reported to be severely defective in vitro failed to support growth of the acpP strain in vivo (or supported only weak growth). A collection of ACPs from diverse bacteria and from three eukaryotic organelles was also tested. All of the bacterial ACPs tested restored growth to the E. coli acpP mutant strain except those from two related bacteria, Enterococcus faecalis and Lactococcus lactis. Only one of the three eukaryotic organellar ACPs allowed growth. Strikingly the ACP is that of the apicoplast of Plasmodium falciparum (the protozoan that causes malaria). The fact that an ACP from a such diverse organism can replace AcpP function in E. coli suggests that some of the protein-protein interactions detected for AcpP may be not be essential for growth of E. coli.

In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis. Publishing Authors By Initials

NR De Lay,JE Cronan,

For similar proteins: protozoan proteins research abstracts see: proteins: protozoan proteins research

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In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 20319-28

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 23

MONTH: 05

YEAR: 2007

In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis. Keywords Mesh Terms:

KEYWORDS: Protozoan Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis. Information

Substance Name: acpP protein, E coli

Registry Number: 0

Grant and Affiliation Information for In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis.

AFFILIATION: Department of Microbiology, University of Illinois at Urbana-Champaign, 601 S. Goodwin Avenue, Urbana, IL 61801, USA.

Country: United States

AGENCY: United States NIAID

GRANT: AI 15650

ACRONYM: AI

MEDLINETA: J Biol Chem

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