Binding of BiP to assembly-defective plant protein (Articolo in rivista)

Type

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

Label

• Binding of BiP to assembly-defective plant protein (Articolo in rivista) (literal)

Anno

• 1994-01-01T00:00:00+01:00 (literal)

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

• 10.1046/j.1365-313X.1994.5010103.x (literal)

Alternative label

• E. Pedrazzini, G. Giovinazzo, R. Bollini, A. Ceriotti and A. Vitale (1994)
  Binding of BiP to assembly-defective plant protein
  in Plant journal (Print)
  (literal)

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

• E. Pedrazzini, G. Giovinazzo, R. Bollini, A. Ceriotti and A. Vitale (literal)

Pagina inizio

• 103 (literal)

Pagina fine

• 110 (literal)

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

• http://onlinelibrary.wiley.com/doi/10.1046/j.1365-313X.1994.5010103.x/abstract (literal)

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

• 5 (literal)

Rivista

• Plant journal (Rivista)

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

• 1 (literal)

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

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

Titolo

• Binding of BiP to assembly-defective plant protein (literal)

Abstract

• The binding protein (BiP) has been implicated as a mediator of protein folding and assembly in the endoplasmic reticulum of mammalian cells and has often been found in stable association with structurally defective proteins. To acquire information on the activity of BiP in plant cells, we have expressed in tobacco protoplasts the wild type form and an assembly-defective form of bean phaseolin. Phaseolin (PHSL) is a soluble, trimeric, storage glycoprotein co-translationally inserted into the lumen of the endoplasmic reticulum and then transported along the secretory pathway to the protein storage vacuoles. We have previously shown that a PHSL mutant in which the last 59 amino acids have been deleted (A363PHSL) is unable to form trimers and is retained in a pre-Golgi compartment when synthesized in Xenopus oocytes. When transiently expressed in tobacco leaf protoplasts, wild-type PHSL is correctly glycosylated and assembles efficiently and rapidly into trimers. A363PHSL is also correctly glycosylated but does not trimerize. Tobacco BiP and A363PHSL are co-immunoselected using either anti-PHSL or anti-BiP antibodies. Under the same conditions, co-immunoselection of BiP with wild-type PHSL is not detectable. The BiP bound to A363PHSL can be released by treatment of the complex with ATP, indicating that the binding is related to the proposed function of BiP in protein folding and assembly in the endoplasmic reticulum. These data indicate that BiP stably binds structurally defective proteins in plant cells. (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

• ALDO CERIOTTI (Persona)
• ROBERTO BOLLINI (Persona)
• ALESSANDRO VITALE (Unità di personale interno)
• GIOVANNA GIOVINAZZO (Unità di personale interno)
• EMANUELA PEDRAZZINI (Unità di personale interno)

Insieme di parole chiave

• Keywords of "Binding of BiP to assembly-defective plant protein" (Insieme di parole chiave)

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

• GIOVANNA GIOVINAZZO (Unità di personale interno)
• ALDO CERIOTTI (Persona)
• EMANUELA PEDRAZZINI (Unità di personale interno)
• ALESSANDRO VITALE (Unità di personale interno)
• ROBERTO BOLLINI (Persona)

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

• Plant journal (Rivista)

Insieme di parole chiave di

• Keywords of "Binding of BiP to assembly-defective plant protein" (Insieme di parole chiave)