A novel C-terminal sequence from barley polyamine oxidase is a vacuolar sorting signal. (Articolo in rivista)

Type

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

Label

• A novel C-terminal sequence from barley polyamine oxidase is a vacuolar sorting signal. (Articolo in rivista) (literal)

Anno

• 2004-01-01T00:00:00+01:00 (literal)

Alternative label

• Cervelli M., Di Caro O., Di Penta A., Angelini R., Federico R., Vitale A., Mariottini P. (2004)
  A novel C-terminal sequence from barley polyamine oxidase is a vacuolar sorting signal.
  in Plant journal (Print)
  (literal)

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

• Cervelli M., Di Caro O., Di Penta A., Angelini R., Federico R., Vitale A., Mariottini P. (literal)

Pagina inizio

• 410 (literal)

Pagina fine

• 418 (literal)

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

• 40 (literal)

Rivista

• Plant journal (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Dipartimento di Biologia, Universita Roma Tre, Rome 1, IBBA-CNR 2 (literal)

Titolo

• A novel C-terminal sequence from barley polyamine oxidase is a vacuolar sorting signal. (literal)

Abstract

• Barley contains two different isoforms of flavin-containing polyamine oxidase (BPAO1 and BPAO2). We havepreviously demonstrated that BPAO2 is a symplastic protein in barley leaves. On the contrary, maizepolyamine oxidase (MPAO), the best characterized member of this enzyme class, is apoplastic. Comparison ofthe derived amino-acid sequences of BPAO2 and MPAO has revealed that both precursor proteins include acleavable N-terminal signal peptide of 25 amino acid residues, but the barley enzyme shows an extraC-terminal extension of eight amino acids. By means of MPAO engineering with BPAO2 C-terminal tail (MPAOT)and exploiting transient expression in Nicotiana tabacum protoplasts, we demonstrate that thisoligopeptide is a signal for protein sorting to the plant vacuole. The vacuolar sorting of MPAO-T wassaturable. Specific mutations of the C-terminal tail were constructed to determine which amino acid residuesof this novel propeptide affect proper protein sorting. No consensus sequence or common structuraldeterminant is required for the intracellular retention of the MPAO-T protein, but a gradual lowering of theefficiency was observed as a result of progressive deletion of the C-terminus. (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 journal (Rivista)