Difference between revisions of "PMID:1649829"

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'''Hsu, L, Jackowski, S and Rock, CO'''  (1991) Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity.''J. Biol. Chem.'' '''266''':13783-8
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!align=left  |Abstract
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2-Acyl-glycerophosphoethanolamine (2-acyl-GPE) acyltransferase and acyl-acyl carrier protein (acyl-ACP) synthetase are thought to be dual catalytic activities of a single inner membrane enzyme. A filter disc replica print method for the detection of acyl-ACP synthetase activity by colony fluorography was used to screen a mutagenized population of cells for acyl-ACP synthetase mutants (aas). All aas mutants lacked both acyl-ACP synthetase and 2-acyl-GPE acyltransferase activities in vitro. There was no detectable acyl-CoA-independent incorporation of exogenous fatty acids into phosphatidylethanolamine or the major outer membrane lipoprotein in aas mutants. Exogenous lysophospholipid uptake and acylation was also lacking in aas mutants. Lipoprotein acylation by phospholipids synthesized by the de novo biosynthetic pathway was not affected in aas mutants showing that this gene product was not directly involved in lipoprotein biogenesis. The aas mutants had an altered membrane phospholipid composition and accumulated both 2-acyl-GPE and acylphosphatidylglycerol. Acylphosphatidylglycerol accumulation was due to the transacylase activity of lysophospholipase L2 (the pldB gene product) since aas pldB double mutants accumulated 2-acyl-GPE, but not acylphosphatidylglycerol. The aas allele was mapped to 61 min of the Escherichia coli chromosome, and the deduced gene order in this region was thyA-aas-lysA. The biochemical, physiological, and genetic analyses of aas mutants support the conclusion that 2-acyl-GPE acyltransferase and acyl-ACP synthetase are two activities of the same protein and confirm that this enzyme system participates in membrane phospholipid turnover and governs the acyl-CoA independent incorporation of exogenous fatty acids and lysophospholipids into the membrane.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1649829 PubMed]
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!align=left  |Keywords
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Acylation; Acyltransferases; Chromosome Mapping; Coenzyme A Ligases; Escherichia coli; Fatty Acids; Genes, Bacterial; Lysophospholipids; Membrane Lipids; Multienzyme Complexes; Mutation; Phosphatidylethanolamines; Phosphotransferases; Proteins; Transferases (Other Substituted Phosphate Groups)
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==Main Points of the Paper ==
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{{LitSignificance}}
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== Materials and Methods Used ==
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{{LitMaterials}}
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==Phenotype Annotations==
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{{AnnotationTableHelp}}
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{|  id="P4d7f9aaa26019"  class=" tableEdit PMID_Phenotype_table" 
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!|Species!!Taxon ID!!Strain!!Gene (if known)!!OMP!!Phenotype!!Details!!Evidence!!Notes
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''Escherichia coli''
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LCH1
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''aas-1''
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abolished acyl-ACP synthetase activity
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''Escherichia coli''
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LCH2
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''aas-2''
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abolished acyl-ACP synthetase activity
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''Escherichia coli''
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LCH1
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''aas-1''
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abolished acyltransferase activity
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Metabolic Activity
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Biochemical Assay
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Table 2
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''Escherichia coli''
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LCH1
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''aas-1''
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*altered composition of phospholipid membrane
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*increased lysophosphatidylethanolamine content in membrane
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Metabolic Activity
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Biochemical Assay
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''Escherichia coli''
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LCH1
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''aas-1''
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*altered composition of phospholipid membrane
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*increased accumulation of Acyl-PtdGro
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Biochemical Assay
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''Escherichia coli''
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LK29
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''pld12''
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*altered membrane composition
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*absent acyl-PtdGro in membranes
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Biochemical Assay
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''Escherichia coli''
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''fadD''
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absent acyl-CoA synthetase activity
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Biochemical Assay
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==Notes==
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==References==
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{{RefHelp}}
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<references/>
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[[Category:Publication]]
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[[Category:To Be Converted]]

Latest revision as of 12:08, 22 June 2011

Citation

Hsu, L, Jackowski, S and Rock, CO (1991) Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity.J. Biol. Chem. 266:13783-8

Abstract

2-Acyl-glycerophosphoethanolamine (2-acyl-GPE) acyltransferase and acyl-acyl carrier protein (acyl-ACP) synthetase are thought to be dual catalytic activities of a single inner membrane enzyme. A filter disc replica print method for the detection of acyl-ACP synthetase activity by colony fluorography was used to screen a mutagenized population of cells for acyl-ACP synthetase mutants (aas). All aas mutants lacked both acyl-ACP synthetase and 2-acyl-GPE acyltransferase activities in vitro. There was no detectable acyl-CoA-independent incorporation of exogenous fatty acids into phosphatidylethanolamine or the major outer membrane lipoprotein in aas mutants. Exogenous lysophospholipid uptake and acylation was also lacking in aas mutants. Lipoprotein acylation by phospholipids synthesized by the de novo biosynthetic pathway was not affected in aas mutants showing that this gene product was not directly involved in lipoprotein biogenesis. The aas mutants had an altered membrane phospholipid composition and accumulated both 2-acyl-GPE and acylphosphatidylglycerol. Acylphosphatidylglycerol accumulation was due to the transacylase activity of lysophospholipase L2 (the pldB gene product) since aas pldB double mutants accumulated 2-acyl-GPE, but not acylphosphatidylglycerol. The aas allele was mapped to 61 min of the Escherichia coli chromosome, and the deduced gene order in this region was thyA-aas-lysA. The biochemical, physiological, and genetic analyses of aas mutants support the conclusion that 2-acyl-GPE acyltransferase and acyl-ACP synthetase are two activities of the same protein and confirm that this enzyme system participates in membrane phospholipid turnover and governs the acyl-CoA independent incorporation of exogenous fatty acids and lysophospholipids into the membrane.

Links

PubMed

Keywords

Acylation; Acyltransferases; Chromosome Mapping; Coenzyme A Ligases; Escherichia coli; Fatty Acids; Genes, Bacterial; Lysophospholipids; Membrane Lipids; Multienzyme Complexes; Mutation; Phosphatidylethanolamines; Phosphotransferases; Proteins; Transferases (Other Substituted Phosphate Groups)

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Main Points of the Paper

Please summarize the main points of the paper.

Materials and Methods Used

Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).

Phenotype Annotations

See Help:AnnotationTable for details on how to edit this table.
<protect>

Species Taxon ID Strain Gene (if known) OMP Phenotype Details Evidence Notes

Escherichia coli

LCH1

aas-1

abolished acyl-ACP synthetase activity

Escherichia coli

LCH2

aas-2

abolished acyl-ACP synthetase activity

Escherichia coli

LCH1

aas-1

abolished acyltransferase activity

Metabolic Activity

Biochemical Assay

Table 2

Escherichia coli

LCH1

aas-1

  • altered composition of phospholipid membrane
  • increased lysophosphatidylethanolamine content in membrane

Metabolic Activity

Biochemical Assay

Escherichia coli

LCH1

aas-1

  • altered composition of phospholipid membrane
  • increased accumulation of Acyl-PtdGro

Biochemical Assay

Escherichia coli

LK29

pld12

  • altered membrane composition
  • absent acyl-PtdGro in membranes

Biochemical Assay

Escherichia coli

fadD

absent acyl-CoA synthetase activity

Biochemical Assay


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</protect>

Notes

References

See Help:References for how to manage references in omp dev.

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