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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0036025,
umls-concept:C0069966,
umls-concept:C0185023,
umls-concept:C0237497,
umls-concept:C0332120,
umls-concept:C0439097,
umls-concept:C0456387,
umls-concept:C1314972,
umls-concept:C1511539,
umls-concept:C1547348,
umls-concept:C1705241,
umls-concept:C1947904,
umls-concept:C1999228,
umls-concept:C2825781
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pubmed:issue |
3
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pubmed:dateCreated |
1994-2-25
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pubmed:abstractText |
Saccharomyces cerevisiae was used as a model system to characterize the covalent attachment of palmitoleic acid to proteins. Chemically synthesized cis-[9,10-3H]hexadecenoic acid (palmitoleic acid) was used to demonstrate the attachment of this lipid species to at least six proteins (m = 122, 58, 45, 41, 31, and 17 kDa). The majority of the labeled proteins are distinct from those labeled with [3H]palmitic acid (16:0). Based on the lability of the bond in the presence of methanolic KOH or hydroxylamine (pH 8), we propose that [3H] palmitoleic acid is attached to proteins via a thioester linkage. The identity of the palmitoleic acid was established by C-18 reverse phase high performance thin layer chromatography and argentation thin layer chromatography analysis after the fatty acid was liberated from the proteins by either transesterification or saponification. Incorporation of [3H]palmitoleic acid into proteins was only slightly inhibited (relative to [3H] myristic acid) by the presence of cycloheximide, indicating that the attachment of [3H]palmitoleic acid occurs post-translationally. This report is the first description of multiprotein acylation by a long chain unsaturated fatty acid.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Monounsaturated,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium,
http://linkedlifedata.com/resource/pubmed/chemical/palmitoleic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2082-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8294460-Acylation,
pubmed-meshheading:8294460-Carbon Radioisotopes,
pubmed-meshheading:8294460-Chromatography, Thin Layer,
pubmed-meshheading:8294460-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8294460-Fatty Acids, Monounsaturated,
pubmed-meshheading:8294460-Fungal Proteins,
pubmed-meshheading:8294460-Molecular Weight,
pubmed-meshheading:8294460-Saccharomyces cerevisiae,
pubmed-meshheading:8294460-Tritium
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pubmed:year |
1994
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pubmed:articleTitle |
Covalent attachment of palmitoleic acid (C16:1 delta 9) to proteins in Saccharomyces cerevisiae. Evidence for a third class of acylated proteins.
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pubmed:affiliation |
Department of Microbiology, North Carolina State University, Raleigh 27695-7615.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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