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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1991-11-15
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pubmed:abstractText |
ras proteins undergo posttranslational modification by a 15-carbon farnesyl isoprenoid at a cysteine within a defined COOH-terminal amino acid motif; i.e., Cys-Ali-Ali-Ser/Met (where Ali represents an aliphatic residue). In other low molecular mass GTP-binding proteins, cysteines are modified by 20-carbon geranylgeranyl groups within a Cys-Ali-Ali-Leu motif. We changed the terminal Ser-189 of Ha-ras p21 to Leu-189 by site-directed mutagenesis and found that the protein was modified by [3H]geranylgeranyl instead of [3H]farnesyl in an in vitro assay. Gel-permeation chromatography of [3H]mevalonate-labeled hydrocarbons released from immunoprecipitated ras proteins overexpressed in COS cells indicated that Ha-ras p21(Leu-189) was also a substrate for 20-carbon isoprenyl modification in vivo. Additional steps in Ha-ras p21 processing, normally initiated by farnesylation, appear to be supported by geranylgeranylation, based on metabolic labeling of Ha-ras p21(Leu-189) with [3H]palmitate and its subcellular localization in a particulate fraction from COS cells. These observations indicate that the amino acid occupying the terminal position (Xaa) in the Cys-Ali-Ali-Xaa motif constitutes a key structural feature by which Ha-ras p21 and other proteins with ras-like COOH-terminal isoprenylation sites are distinguished as substrates for farnesyl- or geranylgeranyltransferases.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-1850747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-1898776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-1899909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-1902099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-1903399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-1921989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-1992464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2018975,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2116010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2116011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2120220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2120222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2123345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2123808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2124698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2180959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2183224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2187294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2194674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2203759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2204115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2217184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2217200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2233726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2296720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2296721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2325650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2385292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2398053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2569235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2661017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2682646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2684976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2686979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-2722778,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-3290900,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-3638306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924354-3996185
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8934-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1924354-Amino Acid Sequence,
pubmed-meshheading:1924354-Animals,
pubmed-meshheading:1924354-Base Sequence,
pubmed-meshheading:1924354-Cell Line,
pubmed-meshheading:1924354-Cysteine,
pubmed-meshheading:1924354-GTP-Binding Proteins,
pubmed-meshheading:1924354-Mevalonic Acid,
pubmed-meshheading:1924354-Molecular Sequence Data,
pubmed-meshheading:1924354-Mutagenesis, Site-Directed,
pubmed-meshheading:1924354-Oligonucleotides,
pubmed-meshheading:1924354-Polyisoprenyl Phosphates,
pubmed-meshheading:1924354-Protein Biosynthesis,
pubmed-meshheading:1924354-Protein Processing, Post-Translational,
pubmed-meshheading:1924354-Proto-Oncogene Proteins p21(ras),
pubmed-meshheading:1924354-Sesquiterpenes,
pubmed-meshheading:1924354-Transfection
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pubmed:year |
1991
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pubmed:articleTitle |
Posttranslational modification of Ha-ras p21 by farnesyl versus geranylgeranyl isoprenoids is determined by the COOH-terminal amino acid.
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pubmed:affiliation |
Weis Center for Research, Geisinger Clinic, Danville, PA 17822.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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