Over-expression of peptide deformylase in chloroplasts confers actinonin resistance, but is not a suitable selective marker system for plastid transformation.

Transgenic Res

Instituto de Agrobiotecnología, Universidad Pública de Navarra-CSIC-Gobierno de Navarra, Campus de Arrosadía, 31006, Pamplona, Spain.

Published: June 2011

AI Article Synopsis

  • The Arabidopsis thaliana peptide deformylase PDF1B was successfully expressed in tobacco chloroplasts and made up 6% of the total soluble protein, proving its enzymatic activity.
  • Transgenic tobacco plants showed resistance to the inhibitor actinonin during seed germination and shoot development.
  • However, using PDF1B and actinonin as the main selection system resulted in all shoots being escapes, indicating this method may only serve as a secondary selection marker in plastid transformation.

Article Abstract

Arabidopsis thaliana peptide deformylase PDF1B was expressed in tobacco chloroplasts using spectinomycin as the selective agent. The foreign protein accumulated in chloroplasts (6% of the total soluble protein) and was enzymatically active. Transplastomic plants were evaluated for resistance to the peptide deformylase inhibitor actinonin. In vitro seed germination in the presence of actinonin and in planta application of the inhibitor demonstrated the resistance of the transformed plants. In addition, transgenic leaf explants were able to develop shoots via organogenesis in the presence of actinonin. However, when the combination of the PDF1B gene and actinonin was used as the primary selective marker system for chloroplast transformation of tobacco, all developed shoots were escapes. Therefore, under the experimental conditions tested, the use of this system for plastid transformation would be limited to function as a secondary selective marker.

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http://dx.doi.org/10.1007/s11248-010-9447-9DOI Listing

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