Expression of the wild-type and mutated vacuolar storage protein phaseolin in Xenopus oocytes reveals relationships between assembly and intracellular transport (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Expression of the wild-type and mutated vacuolar storage protein phaseolin in Xenopus oocytes reveals relationships between assembly and intracellular transport (Articolo in rivista) (literal)

Anno

• 1991-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1111/j.1432-1033.1991.tb16456.x (literal)

Alternative label

• A. Ceriotti, E. Pedrazzini, M.S. Fabbrini, M. Zoppè, R. Bollini, A. Vitale (1991)
  Expression of the wild-type and mutated vacuolar storage protein phaseolin in Xenopus oocytes reveals relationships between assembly and intracellular transport
  in European journal of biochemistry (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• A. Ceriotti, E. Pedrazzini, M.S. Fabbrini, M. Zoppè, R. Bollini, A. Vitale (literal)

Pagina inizio

• 959 (literal)

Pagina fine

• 968 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1991.tb16456.x/full (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 202 (literal)

Rivista

• European journal of biochemistry (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 3 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Consiglio Nazionale delle Ricerche - Istituto di Biologia e Biotecnologia Agraria Milano (literal)

Titolo

• Expression of the wild-type and mutated vacuolar storage protein phaseolin in Xenopus oocytes reveals relationships between assembly and intracellular transport (literal)

Abstract

• The role played by subunit assembly in the intracellular transport of the bean storage protein phaseolin, a soluble trimeric glycoprotein, was investigated using Xenopus oocytes injected with RNA. We show that phaseolin assembly is dependent upon the level of synthesis of the protein and is required for intracellular transport out of the endoplasmic reticulum. We also show that a fraction of the assembled phaseolin is permanently retained in a post-endoplasmic reticulum compartment. Deletion of the C-terminal a-helical domain fully prevents in vivo assembly but not endoplasmic reticulum retention. This indicates that this domain is necessary for trimerization but not for interactions of unassembled subunits with endoplasmic reticulum components. The truncated phaseolin has high in vivo stability. The potential implications of these findings on the possibility to improve the nutritional value of phaseolin through genetic engineering are discussed. (literal)

Prodotto di

• Basi molecolari, fisiologiche e cellulari delle produzioni vegetali. (AG.P01.001.001) (Modulo)
• Institute of agricultural biology and biotechnology (IBBA) (Istituto)

Autore CNR

• ROBERTO BOLLINI (Persona)
• ALDO CERIOTTI (Persona)
• EMANUELA PEDRAZZINI (Unità di personale interno)
• ALESSANDRO VITALE (Unità di personale interno)
• MONICA MARIA ZOPPE' (Unità di personale interno)

Incoming links:

Prodotto

• Institute of agricultural biology and biotechnology (IBBA) (Istituto)
• Basi molecolari, fisiologiche e cellulari delle produzioni vegetali. (AG.P01.001.001) (Modulo)

Autore CNR di

• ALDO CERIOTTI (Persona)
• EMANUELA PEDRAZZINI (Unità di personale interno)
• ALESSANDRO VITALE (Unità di personale interno)
• ROBERTO BOLLINI (Persona)
• MONICA MARIA ZOPPE' (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• European journal of biochemistry (Rivista)