Plant Molecular Biology

, Volume 69, Issue 5, pp 517–528

A protein related to prokaryotic UMP kinases is involved in psaA/B transcript accumulation in Arabidopsis


  • Paul Hein
    • Institute of General Botany and Plant PhysiologyFriedrich-Schiller-Universität Jena
  • Jana Stöckel
    • Department of BiologyWashington University
  • Stefan Bennewitz
    • Department of BiologyWashington University
    • Institute of General Botany and Plant PhysiologyFriedrich-Schiller-Universität Jena

DOI: 10.1007/s11103-008-9433-2

Cite this article as:
Hein, P., Stöckel, J., Bennewitz, S. et al. Plant Mol Biol (2009) 69: 517. doi:10.1007/s11103-008-9433-2


Dpt1 (defect inpsaA/Btranscript accumulation 1) is a novel photosystem (PS) I mutant in Arabidopsis. dpt1 mutants fail to grow photoautotrophically, and are impaired in the accumulation of psaA/B transcripts while the transcript levels for the remaining PSI subunits, for subunits of the PSII, the cyt-b6/f-complex, and the ribulose-1,5-bisphosphate carboxylase are comparable to the wild type. In-organello run-on transcription assays demonstrate that the lower psaA/B transcript abundance in dpt1-1 is not caused by the inability to transcribe the psaA/psaB/rps14 operon. psaA/B transcripts in the mutant are associated with polyribosomes and translated. Thus, the mutation affects post-transcriptional processes specific for psaA/B. The dpt1 gene was isolated by map-based cloning. The protein is localized in the stroma of the chloroplast and exhibits striking similarities to UMP kinases of prokaryotic origin. Our results show that the nuclear encoded protein Dpt1 is essential for retaining photosynthetic activity in higher plant chloroplasts and involved in post-transcriptional steps of psaA/B transcript accumulation. We discuss that Dpt1 may be a bifunctional protein that couples the pyrimidine metabolism to the photosynthetic electron transport.


ArabidopsisChloroplastGene expressionPhotosystem IMap-based cloning



Defect in psaA/B transcript accumulation 1


Photosystem I


Uridine monophosphate

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© Springer Science+Business Media B.V. 2008