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Published on December 27, 2007; 10.1104/pp.107.114702


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Received December 7, 2007
Accepted December 21, 2007

Functions of chloroplastic adenylate kinases in Arabidopsis thaliana

Peter Robert Lange , Claudia Geserick , Gilbert Tischendorf , and Rita Zrenner *

Max-Planck-Institut fur Molekulare Pflanzenphysiologie, Am Muhlenberg 1, 14476 Golm, Germany; Freie Universitat Berlin, Institut fur Biologie, Pflanzenphysiologie, Konigin-Luise-Str. 12-16, 14195 Berlin, Germany

* Corresponding author; email: zrenner{at}mpimp-golm.mpg.de.

Adenosine monophosphate kinase (AMK, adenylate kinase) catalyses the reversible formation of ADP by the transfer of one phosphate group from ATP to AMP, thus equilibrating adenylates. The Arabidopsis genome contains 10 genes with an adenylate/cytidylate kinase signature; seven of these are identified as putative adenylate kinases. Encoded proteins of at least two members of this Arabidopsis adenylate kinase gene family are targeted to plastids. However, when the individual genes are disrupted the phenotypes of both mutants are strikingly different. Although absence of AMK2 causes only 30% reduction of total adenylate kinase activity in leaves there is loss of chloroplast integrity leading to small, pale looking plantlets from embryo through to seedling development. In contrast, no phenotype for disruption of the second plastid adenylate kinase was found. From this analysis we conclude that AMK2 is the major activity for equilibration of adenylates and de novo synthesis of ADP in the plastid stroma.







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