C-terminal extension of phaseolin with a short methionine-rich sequence can inhibit trimerisation and result in high instability (Articolo in rivista)

Type

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

Label

• C-terminal extension of phaseolin with a short methionine-rich sequence can inhibit trimerisation and result in high instability (Articolo in rivista) (literal)

Anno

• 2003-01-01T00:00:00+01:00 (literal)

Alternative label

• Nuttall J., Vitale A., Frigerio, L. (2003)
  C-terminal extension of phaseolin with a short methionine-rich sequence can inhibit trimerisation and result in high instability
  in Plant molecular biology
  (literal)

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

• Nuttall J., Vitale A., Frigerio, L. (literal)

Pagina inizio

• 885 (literal)

Pagina fine

• 894 (literal)

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

• 51 (literal)

Rivista

• Plant molecular biology (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• C-terminal extension of phaseolin with a short methionine-rich sequence can inhibit trimerisation and result in high instability (literal)

Abstract

• In an attempt to increase the content in essential amino acids methionine and tryptophan of the trimeric storage protein phaseolin, we fused a Met- and Trp-rich sequence to the C-terminus of a phaseolin variant lacking its vacuolar sorting signal, with the aim to target the protein for secretion and accumulation into the apoplast. The fate of the mutant protein, denominated Y3, was studied in transiently transfected tobacco protoplasts. We report that the presence of the additional sequence causes structural defects which inhibit trimerization and lead to partial aggregation of Y3. The protein interacts with the ER chaperone BiP prior to being degraded very rapidly, in a process that does not require vesicular transport from the ER. The rate of degradation of Y3 is higher than that observed for another assembly defective mutant of phaseolin, delta360, which remains monomeric and does not aggregate. This indicates that the plant ER quality control machinery can dispose of defective proteins with different kinetics and perhaps mechanisms, depending on the nature of their defect. (literal)

Prodotto di

• Institute of agricultural biology and biotechnology (IBBA) (Istituto)

Autore CNR

• ALESSANDRO VITALE (Unità di personale interno)

Incoming links:

Prodotto

• Institute of agricultural biology and biotechnology (IBBA) (Istituto)

Autore CNR di

• ALESSANDRO VITALE (Unità di personale interno)

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

• Plant molecular biology (Rivista)