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Post-translational processing of the amino terminus affects actin function.
Hennessey, E S; Drummond, D R; Sparrow, J C.
Afiliación
  • Hennessey ES; Department of Biology, University of York, England.
Eur J Biochem ; 197(2): 345-52, 1991 Apr 23.
Article en En | MEDLINE | ID: mdl-1902786
We have studied the importance of N-terminal processing for normal actin function using the Drosophila Act88F actin gene transcribed and translated in vitro. Despite having different charges as determined by two-dimensional (2D) gel electrophoresis, Act88F expressed in vivo and in vitro in rabbit reticulocyte lysate bind to DNase I with equal affinity and are able to copolymerise with bulk rabbit actin equally well. Using peptide mapping and thin-layer electrophoresis we have shown that bestatin [( 3-amino-2-hydroxy-4-phenyl-butanoyl]-L-leucine), an inhibitor of aminopeptidases, can inhibit actin N-terminal processing in rabbit reticulocyte lysate. Although processed and unprocessed actins translated in vitro are able to bind to DNase I equally well, unprocessed actins are less able to copolymerise with bulk actins. This effect is more pronounced when bulk rabbit actin is used but is still seen with bulk Lethocerus actin. Also, the unprocessed actins reduce the polymerisation of the processed actin translated in vitro with the bulk rabbit actin. This suggests that individual actins do interact, even in non-polymerising conditions. The reduced ability of unprocessed actin to polymerise shows that correct post-translational modification of the N terminus is required for normal actin function.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Actinas / Drosophila melanogaster Límite: Animals Idioma: En Revista: Eur J Biochem Año: 1991 Tipo del documento: Article País de afiliación: Reino Unido Pais de publicación: Reino Unido
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Procesamiento Proteico-Postraduccional / Actinas / Drosophila melanogaster Límite: Animals Idioma: En Revista: Eur J Biochem Año: 1991 Tipo del documento: Article País de afiliación: Reino Unido Pais de publicación: Reino Unido