http://www.cnr.it/ontology/cnr/individuo/prodotto/ID110841
Localization of the recombinant protein zeolin in the chloroplast. (Abstract/Poster in atti di convegno)
- Type
- Label
- Localization of the recombinant protein zeolin in the chloroplast. (Abstract/Poster in atti di convegno) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Alternative label
De Marchis F, Bellucci M, Arcioni S (2006)
Localization of the recombinant protein zeolin in the chloroplast.
in 50° Annual Congress of the Italian Society of Agriculture Genetics, Ischia-Italia, 10/09/2006
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- De Marchis F, Bellucci M, Arcioni S (literal)
- Note
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Genetica Vegetale, Unità Organizzativa di Supporto di Perugia, CNR, via della Madonna Alta, 130, 06128 Perugia. (literal)
- Titolo
- Localization of the recombinant protein zeolin in the chloroplast. (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#isbn
- Abstract
- Plants are potentially useful for the production of many therapeutic proteins and several
strategies have been exploited to maximize heterologous protein accumulation in the plant cell.
Recently, a fusion protein made between the bean storage protein phaseolin and the N-terminal
portion of maize prolamin storage protein ?-zein was shown to accumulate in novel ER-derived
protein bodies of vegetative tissues, while ?-zein and phaseolin usually accumulates in the ER and
in storage vacuoles respectively. The ?-zein fragment, on the basis of the knowledge acquired on
zeolin, could be exploited for the production of large amounts of recombinant pharmaceuticals in
transgenic plants. In this study we investigate if zeolin could be also expressed in the chloroplast
and not only in the ER. In fact, together with others numerous advantages such as high-level of
transgene expression, in many crop species chloroplast DNA is not transmitted through pollen thus
eliminating the risk of transgene spreading in not transgenic crops or relative wild species. The
zeolin gene has been cloned in three plastid expression cassettes. Two of them have been assembled
to evaluate the utility of including in the zeolin gene the region that encodes the signal peptide. In
the third construct the BiP gene, which encodes an ER chaperone, has been cloned downstream of
the zeolin gene. The presence of the signal peptide seems to promote zeolin accumulation in the
chloroplast, even though a comparison between the two zeolin sub-cellular localizations shows that
zeolin has accumulated in the chloroplast to lower levels than in the ER. Immunoblotting of the
transplastomic plant protein shows the considerable presence of phaseolin and ?-zein polypeptides
with respect to intact zeolin. This suggests that in the chloroplast a higher amount of zeolin is
fragmented in comparison to zeolin accumulated in the ER. Moreover, no protein bodies have been
detected in the chloroplast. In order to promote zeolin folding into protein bodies in this organelle,
we have integrated the BiP gene together with the zeolin gene in the tobacco plastome but even in
this case transplastomic plants has not accumulated zeolin in protein bodies. We hypothesize that
the disulfide bonds necessary for zeolin assembly have not been correctly formed in the chloroplast.
This can have caused zeolin misfolding and not-stable proteins that reach poor expression levels
due to chloroplast proteases activity. (literal)
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- Autore CNR
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