Binding of GDP to a ribosomal protein after elongation factor-2 dependent GTP hydrolysis.
Biochim Biophys Acta
; 1132(3): 284-9, 1992 Oct 20.
Article
em En
| MEDLINE
| ID: mdl-1420308
ABSTRACT
Incubation of 80S ribosomes with a substoichiometric amount of [alpha-32P]GTP and with eEF-2 resulted in the specific labeling of one ribosomal protein which migrated very close to the position of the acidic phosphoprotein P2 from the 60S subunit in two-dimensional isofocusing-SDS gel electrophoresis. Localization of protein P2 in this electrophoretic system was ascertained by correlation with its position in the standard two-dimensional acidic-SDS gel electrophoresis after its specific phosphorylation by casein kinase II. Labeling of the ribosomal protein was dependent on the presence of eEF-2, and could be attributed to [alpha-32P]GDP binding from the results of chase experiments and HPLC identification, this binding being very likely responsible for the slight shift in the electrophoretical position of the protein. Incubation of ribosomes with tRNA(Phe) in the absence of mRNA induced the release of the bound GDP.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Ribossômicas
/
Fatores de Alongamento de Peptídeos
/
Guanosina Difosfato
/
Guanosina Trifosfato
Idioma:
En
Ano de publicação:
1992
Tipo de documento:
Article