A plant secretory signal peptide targets plastome-encoded recombinant proteins to the thylakoid (Articolo in rivista)

Type
Label
  • A plant secretory signal peptide targets plastome-encoded recombinant proteins to the thylakoid (Articolo in rivista) (literal)
Anno
  • 2011-01-01T00:00:00+01:00 (literal)
Alternative label
  • De Marchis Francesca; Pompa Andrea; Mannucci Roberta; Morosinotto Tomas; Bellucci Michele; (2011)
    A plant secretory signal peptide targets plastome-encoded recombinant proteins to the thylakoid
    in Plant molecular biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • De Marchis Francesca; Pompa Andrea; Mannucci Roberta; Morosinotto Tomas; Bellucci Michele; (literal)
Pagina inizio
  • 427 (literal)
Pagina fine
  • 441 (literal)
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  • 76 (literal)
Rivista
Note
  • PubMe (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • De Marchis Francesca; Istituto di Genetica Vegetale, Consiglio Nazionale delle Ricerche (CNR), via della Madonna Alta 130, 06128 Perugia, Italy Pompa Andrea; Istituto di Genetica Vegetale, Consiglio Nazionale delle Ricerche (CNR), via della Madonna Alta 130, 06128 Perugia, Italy Mannucci Roberta; Istituto di Medicina Interna, Università di Perugia, Perugia, Italy Morosinotto Tomas; Dipartimento di Biologia, Università degli Studi di Padova, 35121, Padova, Italy Bellucci Michele; Istituto di Genetica Vegetale, Consiglio Nazionale delle Ricerche (CNR), via della Madonna Alta 130, 06128 Perugia, Italy (literal)
Titolo
  • A plant secretory signal peptide targets plastome-encoded recombinant proteins to the thylakoid (literal)
Abstract
  • Plastids are considered promising bioreactors for the production of recombinant proteins, but the knowledge of the mechanisms regulating foreign protein folding, targeting, and accumulation in these organelles is still incomplete. Here we demonstrate that a plant secretory signal peptide is able to target a plastome-encoded recombinant protein to the thylakoid membrane. The fusion protein zeolin with its native signal peptide expressed by tobacco (Nicotiana tabacum) transplastomic plants was directed into the chloroplast thylakoid membranes, whereas the zeolin mutant devoid of the signal peptide, ?zeolin, is instead accumulated in the stroma. We also show that zeolin folds in the thylakoid membrane where it accumulates as trimers able to form disulphide bonds. Disulphide bonds contribute to protein accumulation since zeolin shows a higher accumulation level with respect to stromal ?zeolin, whose folding is hampered as the protein accumulates at low amounts in a monomeric form and it is not oxidized. Thus, post-transcriptional processes seem to regulate the stability and accumulation of plastid-synthesized zeolin. The most plausible zeolin targeting mechanism to thylakoid is discussed herein. (literal)
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