Linked Life Data

2123345

Source:http://linkedlifedata.com/resource/pubmed/id/2123345

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
1991-1-10
pubmed:abstractText
smg p21A and -B are small GTP-binding proteins that share putative effector and consensus C-terminal sequences with ras p21 proteins. In the present report, we showed that human platelet smg p21B became labeled when intact platelets were incubated with exogenous [3H]mevalonolactone and when a purified preparation of smg p21B was incubated with bovine brain membranes and S-adenosyl-L-[methyl-3H]methionine. In addition, we demonstrated by gas chromatography/mass spectrometry that treatment of smg p21B with Raney nickel released a geranylgeranyl moiety in a molar ratio of about 1:1. In contrast, treatment of smg p21B with NH2OH or KOH yielded no evidence for the presence of a palmitoyl thioester. Extensive digestion of smg p21B with Achromobacter protease I yielded two C-terminal tripeptides that contained serine and cysteine in a molar ratio of 2:1. Both peptides were modified by a thioether-linked geranylgeranyl group. One of the peptides comigrated with a 3H-labeled proteolytic product of methylated smg p21B on reverse-phase HPLC and this peptide appeared at the same retention time as that of the other peptide after being treated with KOH. Since the cDNA-predicted C-terminal sequence of smg p21B contains a unique Ser-Ser-Cys peptide within its C-terminal domain, -Lys-Lys-Ser-Ser-Cys-Gln-Leu-Leu184, these results indicate that smg p21B is posttranslationally modified by geranylgeranylation of Cys-181 and suggest that further modifications cause proteolytic removal of the three predicted C-terminal amino acids followed by partial methylation of the cysteinyl carboxyl group.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-17790543, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2105724, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2111441, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2116010, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2116011, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2158984, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2164710, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2183224, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2187294, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2194674, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2325650, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2385292, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2406252, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2492285, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2499046, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2504724, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2511199, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2535967, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2539152, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2542301, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2551287, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2642744, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2661017, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2663468, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2682646, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2684976, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-2849942, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-3045729, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-3056940, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-3137530, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-3143720, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-3144274, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-3290900, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-3304147, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-4213668, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-6438626, http://linkedlifedata.com/resource/pubmed/commentcorrection/2123345-942051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8960-4
pubmed:dateRevised
2010-9-9
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Posttranslationally processed structure of the human platelet protein smg p21B: evidence for geranylgeranylation and carboxyl methylation of the C-terminal cysteine.
pubmed:affiliation
Department of Biochemistry, Kobe University School of Medicine, Japan.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't