Document Detail

The acyl-acyl carrier protein synthetase from Synechocystis sp. PCC 6803 mediates fatty acid import.
MedLine Citation:
PMID:  22535424     Owner:  NLM     Status:  MEDLINE    
The transfer of fatty acids across biological membranes is a largely uncharacterized process, although it is essential at membranes of several higher plant organelles like chloroplasts, peroxisomes, or the endoplasmic reticulum. Here, we analyzed loss-of-function mutants of the unicellular cyanobacterium Synechocystis sp. PCC 6803 as a model system to circumvent redundancy problems encountered in eukaryotic organisms. Cells deficient in the only cytoplasmic Synechocystis acyl-acyl carrier protein synthetase (SynAas) were highly resistant to externally provided α-linolenic acid, whereas wild-type cells bleached upon this treatment. Bleaching of wild-type cells was accompanied by a continuous increase of α-linolenic acid in total lipids, whereas no such accumulation could be observed in SynAas-deficient cells (Δsynaas). When SynAas was disrupted in the tocopherol-deficient, α-linolenic acid-hypersensitive Synechocystis mutant Δslr1736, double mutant cells displayed the same resistance phenotype as Δsynaas. Moreover, heterologous expression of SynAas in yeast (Saccharomyces cerevisiae) mutants lacking the major yeast fatty acid import protein Fat1p (Δfat1) led to the restoration of wild-type sensitivity against exogenous α-linolenic acid of the otherwise resistant Δfat1 mutant, indicating that SynAas is functionally equivalent to Fat1p. In addition, liposome assays provided direct evidence for the ability of purified SynAas protein to mediate α-[(14)C]linolenic acid retrieval from preloaded liposome membranes via the synthesis of [(14)C]linolenoyl-acyl carrier protein. Taken together, our data show that an acyl-activating enzyme like SynAas is necessary and sufficient to mediate the transfer of fatty acids across a biological membrane.
Simon von Berlepsch; Hans-Henning Kunz; Susanne Brodesser; Patrick Fink; Kay Marin; Ulf-Ingo Flügge; Markus Gierth
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-04-24
Journal Detail:
Title:  Plant physiology     Volume:  159     ISSN:  1532-2548     ISO Abbreviation:  Plant Physiol.     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-06-04     Completed Date:  2012-10-09     Revised Date:  2013-06-25    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  606-17     Citation Subset:  IM    
Department of Botany II, University of Cologne, Cologne, Germany.
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MeSH Terms
Bacterial Proteins / genetics,  metabolism*
Biological Transport
Carbon-Sulfur Ligases / genetics,  metabolism*
DNA, Bacterial / genetics
Drug Resistance
Electron Transport
Enzyme Activation
Enzyme Assays
Escherichia coli / genetics,  metabolism
Fatty Acid Transport Proteins / genetics
Homologous Recombination
Liposomes / metabolism
Microbial Viability
Microscopy, Electron, Scanning
Organisms, Genetically Modified / genetics,  metabolism
Saccharomyces cerevisiae / genetics,  metabolism
Saccharomyces cerevisiae Proteins / genetics
Substrate Specificity
Synechocystis / drug effects,  enzymology*,  genetics,  ultrastructure
Time Factors
alpha-Linolenic Acid / metabolism*,  pharmacology
alpha-Tocopherol / metabolism
Reg. No./Substance:
0/Bacterial Proteins; 0/DNA, Bacterial; 0/FAT1 protein, S cerevisiae; 0/Fatty Acid Transport Proteins; 0/Liposomes; 0/Saccharomyces cerevisiae Proteins; 463-40-1/alpha-Linolenic Acid; 59-02-9/alpha-Tocopherol; EC 6.2.-/Carbon-Sulfur Ligases; EC ligase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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