Redox modulation of the expression of bacterial genes encoding cysteine-rich proteins in plant protoplasts

Piñeiro Galvin, Manuel; García Olmedo, Francisco y Diaz Rodriguez, Isabel (1994). Redox modulation of the expression of bacterial genes encoding cysteine-rich proteins in plant protoplasts. "Proceedings of the National Academy of Sciences", v. 91 (n. 9); pp. 3867-3871. ISSN 0027-8424.

Descripción

Título: Redox modulation of the expression of bacterial genes encoding cysteine-rich proteins in plant protoplasts
Autor/es:
  • Piñeiro Galvin, Manuel
  • García Olmedo, Francisco
  • Diaz Rodriguez, Isabel
Tipo de Documento: Artículo
Título de Revista/Publicación: Proceedings of the National Academy of Sciences
Fecha: Abril 1994
Volumen: 91
Materias:
Escuela: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Departamento: Biotecnologia [hasta 2014]
Licencias Creative Commons: Reconocimiento - Sin obra derivada - No comercial

Texto completo

[img]
Vista Previa
PDF (Document Portable Format) - Se necesita un visor de ficheros PDF, como GSview, Xpdf o Adobe Acrobat Reader
Descargar (958kB) | Vista Previa

Resumen

Activity of neomycin phosphotransferase II (NPTII; gene, neo; five cysteines) in tobacco protoplasts transfected with fusions of the octopine TR2' or cauliflower mosaic virus 35S promoter and the neo gene, with or without a signal peptide, increased up to 8-fold in response to externally added dithiothreitol at concentrations that did not affect protoplast viability (up to 2.5 mM). Activity of phosphinothricin acetyltransferase (PAT; gene, bar; one cysteine) expressed under control of the TR1' or 35S promoter was not similarly affected, thus excluding a redox modulation of transcription as the mechanism of NPTII activation by dithiothreitol. Western-blot analyses showed an increase in the amount of protein in response to dithiothreitol, whereas neither the steady-state level of NPTII mRNA nor the specific activity of the purified enzyme was affected. The same type of modulation was observed for transiently expressed beta-glucuronidase (nine cysteines) produced from a fusion with the 35S promoter, with or without a signal peptide. Limitation of cotranslational and/or early posttranslational steps by excessively oxidizing sulfhydryl/disulfide redox potentials is postulated to explain the low net accumulation of cysteine-rich proteins of bacterial origin (i.e., NPTII and beta-glucuronidase) when expressed in plant protoplasts, and the marked increase in such proteins in response to externally added dithiothreitol

Más información

ID de Registro: 5864
Identificador DC: http://oa.upm.es/5864/
Identificador OAI: oai:oa.upm.es:5864
URL Oficial: http://www.pnas.org/content/91/9.toc
Depositado por: Memoria Investigacion
Depositado el: 02 Feb 2011 11:14
Ultima Modificación: 20 Abr 2016 14:34
  • Open Access
  • Open Access
  • Sherpa-Romeo
    Compruebe si la revista anglosajona en la que ha publicado un artículo permite también su publicación en abierto.
  • Dulcinea
    Compruebe si la revista española en la que ha publicado un artículo permite también su publicación en abierto.
  • Recolecta
  • e-ciencia
  • Observatorio I+D+i UPM
  • OpenCourseWare UPM