Linked Life Data

16906759

Source:http://linkedlifedata.com/resource/pubmed/id/16906759

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
2006-8-15
pubmed:abstractText
The gene encoding the unique soluble acyl-acyl carrier protein synthetase (AasS) of the bioluminescent Vibrio harveyi strain B392 has been isolated by expression cloning in Escherichia coli. This enzyme catalyzes the ATP-dependent acylation of the thiol of acyl carrier protein (ACP) with fatty acids with chain lengths from C4 to C18. The gene (called aasS) encodes a protein of 60 kDa, a hexahistidine-tagged version of which was readily expressed in E. coli and purified in large quantities. Surprisingly, the sequence of the encoded protein was significantly more similar to that of an acyl-CoA synthetase of the distantly related bacterium, Thermus thermophilus, than to that of the membrane-bound acyl-acyl carrier protein synthetase of E. coli, an enzyme that catalyzes the same reaction from a more closely related organism. Indeed, the AasS sequence can readily be modeled on the known crystal structures of the T. thermophilus acyl-CoA synthetase with remarkably high levels of conservation of the catalytic site residues. To test the possible role of AasS in the fatty aldehyde-dependent bioluminescence pathway of V. harveyi, the chromosomal aasS gene of the organism was disrupted by insertion of a kanamycin cassette by homologous recombination. The resulting aasS::kan strains retained low levels of acyl-acyl carrier protein synthetase consistent with prior indications of a second such activity in this bacterium. The mutant strains grew normally and had normal levels of bioluminescence but were deficient in the incorporation of exogenous octanoic acid into the cellular phospholipids of V. harveyi, particularly at low octanoate concentrations. These data indicate that AasS is responsible for a high-affinity and high-capacity uptake system that efficiently converts exogenous fatty acids into acyl-ACP species competent to enter the fatty acid biosynthetic cycle.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10008-19
pubmed:dateRevised
2010-1-28
pubmed:meshHeading
pubmed-meshheading:16906759-Aldehydes, pubmed-meshheading:16906759-Base Sequence, pubmed-meshheading:16906759-Binding Sites, pubmed-meshheading:16906759-Carbon-Sulfur Ligases, pubmed-meshheading:16906759-Coenzyme A Ligases, pubmed-meshheading:16906759-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:16906759-Escherichia coli, pubmed-meshheading:16906759-Fatty Acids, pubmed-meshheading:16906759-Luminescent Measurements, pubmed-meshheading:16906759-Membrane Proteins, pubmed-meshheading:16906759-Molecular Sequence Data, pubmed-meshheading:16906759-Molecular Weight, pubmed-meshheading:16906759-Mutation, pubmed-meshheading:16906759-Saccharomyces cerevisiae Proteins, pubmed-meshheading:16906759-Substrate Specificity, pubmed-meshheading:16906759-Thermus thermophilus, pubmed-meshheading:16906759-Vibrio
pubmed:year
2006
pubmed:articleTitle
The soluble acyl-acyl carrier protein synthetase of Vibrio harveyi B392 is a member of the medium chain acyl-CoA synthetase family.
pubmed:affiliation
Department of Microbiology, University of Illinois, Urbana, Illinois 61801, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural