REVIEW ARTICLE
High Stability of Recombinant Proteins Expressed in Tobacco Chloroplasts
Andrea Molina, Jon Veramendi*
Article Information
Identifiers and Pagination:
Year: 2009Volume: 3
First Page: 67
Last Page: 72
Publisher ID: TOBIOTJ-3-67
DOI: 10.2174/1874070700903010067
Article History:
Received Date: 26/02/2009Revision Received Date: 06/05/2009
Acceptance Date: 26/05/2009
Electronic publication date: 16/7/2009
Collection year: 2009
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: (https://creativecommons.org/licenses/by/4.0/legalcode). This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
The green fluorescent protein and the non-toxic subunit of cholera toxin were expressed in tobacco chloroplasts. Both recombinant proteins accumulated to levels greater than 20% of the total soluble protein. We did not observe light-dependent induction of gene expression despite employing the promoter and 5´-UTR from the psbA gene. Both proteins were stable in young and old leaves. The estimated half-life, determined by pulse-chase labeling, was greater than 48 h. Freeze-drying of pulverized leaves supplied an easy method of post-harvest handling with no significant loss of the recombinant protein after 7 months of storage at room temperature. These data suggest that both proteins are good candidates for the expression of fusion proteins (e.g. with antigens) in tobacco chloroplasts.