Linked Life Data

1556134

Source:http://linkedlifedata.com/resource/pubmed/id/1556134

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1992-5-4
pubmed:abstractText
Heterotrimeric guanine nucleotide-binding proteins are composed of alpha and beta gamma subunits and couple a variety of cell-surface receptors to intracellular enzymes or ion channels. The heterotrimer dissociates into alpha and beta gamma subunits when the alpha subunit is activated by guanine nucleoside triphosphates. Several lines of evidence show that the amino terminus of the alpha subunit is important for the interaction with the beta gamma subunit (Neer, E. J., Pulsifer, L., and Wolf, L. G. (1988) J. Biol. Chem. 263, 8996-9000; Fung, B. K.-K., and Nash, C. R. (1983) J. Biol. Chem. 258, 10503-10510). We have mutagenized the amino terminus of alpha o to dissect the relative contributions of amino-terminal myristoylation and specific amino acid sequences to subunit interaction. Wild-type and mutant alpha o cDNAs were translated in vitro in a rabbit reticulocyte lysate. All proteins were able to bind guanosine 5'-(gamma-thio)triphosphate and to achieve the necessary conformation for protection from tryptic digestion. Two assays of alpha o beta gamma interactions were used: sucrose density gradients to look for stable heterotrimer formation and ADP-ribosylation by pertussis toxin to detect weak or transient alpha o beta gamma interactions. Our results indicate that myristoylation is essential for stable heterotrimer formation, but that nonmyristoylated proteins are also capable of interacting with the beta gamma subunit. Amino acids 7-10 have an important role in alpha o beta gamma interactions whether alpha o is myristoylated or not. Deletion of this region diminishes the ability of alpha o to interact with the beta gamma subunit, but substitutions at this position indicate that other amino acids can be tolerated without affecting subunit interaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6272-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1556134-Adenosine Diphosphate Ribose, pubmed-meshheading:1556134-Amino Acid Sequence, pubmed-meshheading:1556134-Animals, pubmed-meshheading:1556134-Cattle, pubmed-meshheading:1556134-Centrifugation, Density Gradient, pubmed-meshheading:1556134-GTP-Binding Proteins, pubmed-meshheading:1556134-Guanosine 5'-O-(3-Thiotriphosphate), pubmed-meshheading:1556134-Humans, pubmed-meshheading:1556134-Macromolecular Substances, pubmed-meshheading:1556134-Mice, pubmed-meshheading:1556134-Molecular Sequence Data, pubmed-meshheading:1556134-Mutagenesis, Site-Directed, pubmed-meshheading:1556134-Myristic Acid, pubmed-meshheading:1556134-Myristic Acids, pubmed-meshheading:1556134-Peptide Mapping, pubmed-meshheading:1556134-Pertussis Toxin, pubmed-meshheading:1556134-Polymerase Chain Reaction, pubmed-meshheading:1556134-Protein Biosynthesis, pubmed-meshheading:1556134-RNA, Messenger, pubmed-meshheading:1556134-Rabbits, pubmed-meshheading:1556134-Rats, pubmed-meshheading:1556134-Reticulocytes, pubmed-meshheading:1556134-Sequence Homology, Nucleic Acid, pubmed-meshheading:1556134-Transcription, Genetic, pubmed-meshheading:1556134-Virulence Factors, Bordetella
pubmed:year
1992
pubmed:articleTitle
Mutagenesis of the amino terminus of the alpha subunit of the G protein Go. In vitro characterization of alpha o beta gamma interactions.
pubmed:affiliation
Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't