Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-2-25
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2082-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Covalent attachment of palmitoleic acid (C16:1 delta 9) to proteins in Saccharomyces cerevisiae. Evidence for a third class of acylated proteins.
pubmed:affiliation
Department of Microbiology, North Carolina State University, Raleigh 27695-7615.
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