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Plant Physiol, April 2001, Vol. 125, pp. 1912-1918

Chloroplast and Mitochondrial Proteases in Arabidopsis. A Proposed Nomenclature1

Zach Adam,* Iwona Adamska, Kazumi Nakabayashi, Oren Ostersetzer, Kirsten Haussuhl, Andrea Manuell, Bo Zheng, Olivier Vallon, Steven R. Rodermel, Kazuo Shinozaki, and Adrian K. Clarke

Department of Agricultural Botany, The Hebrew University of Jerusalem, Rehovot 76100, Israel (Z.A., O.O.); Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, S-10691 Stockholm, Sweden (I.A., K.H.); Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, Bunkyo-ku, Tokyo, 113-0033 Japan (K.N.); Department of Botany, Iowa State University, Ames, Iowa 50011 (A.M., S.R.R.); Department of Plant Physiology, University of Umeå, S-901 87 Umeå, Sweden (B.Z.); Institut de Biologie Physico-Chimique, Centre National de la Recherche Scientifique, Unité Propre de Recherche 1261, F-75005 Paris, France (O.V.); Laboratory of Plant Molecular Biology, The Institute of Physical and Chemical Research, Koyadai, Tsukuba, Ibaraki, 305-0074 Japan (K.S.); and Botanical Institute, Göteborg University, S-405 30 Göteborg, Sweden (A.K.C).

The identity and scope of chloroplast and mitochondrial proteases in higher plants has only started to become apparent in recent years. Biochemical and molecular studies suggested the existence of Clp, FtsH, and DegP proteases in chloroplasts, and a Lon protease in mitochondria, although currently the full extent of their role in organellar biogenesis and function remains poorly understood. Rapidly accumulating DNA sequence data, especially from Arabidopsis, has revealed that these proteolytic enzymes are found in plant cells in multiple isomeric forms. As a consequence, a systematic approach was taken to catalog all these isomers, to predict their intracellular location and putative processing sites, and to propose a standard nomenclature to avoid confusion and facilitate scientific communication. For the Clp protease most of the ClpP isomers are found in chloroplasts, whereas one is mitochondrial. Of the ATPase subunits, the one ClpD and two ClpC isomers are located in chloroplasts, whereas both ClpX isomers are present in mitochondria. Isomers of the Lon protease are predicted in both compartments, as are the different forms of FtsH protease. DegP, the least characterized protease in plant cells, has the most number of isomers and they are predicted to localize in several cell compartments. These predictions, along with the proposed nomenclature, will serve as a framework for future studies of all four families of proteases and their individual isomers.

1 This work was supported in part by the Israel Science Foundation, by the U.S.-Israel Binational Agricultural Research and Development Fund, and by the U.S.-Israel Binational Science Foundation (grants to Z.A.); by the Carl Tryggers Foundation for Scientific Research, by the Swedish Natural Science Research Council, and by the Swedish Strategic Foundation (grants to I.A.); by the Japan Society for the Promotion of Science (grant to K.N.); by the Ekströms Fellowship of the Stockholm University (grant to K.H.); and by the Swedish Agricultural and Forestry Resource Council, by the Carl Tryggers Foundation for Scientific Research, and by the Swedish Foundation for International Cooperation in Research and Higher Education (grants to A.K.C.)

* Corresponding author; e-mail zach{at}agri.huji.ac.il; fax 972-8-946-7763.

© 2001 American Society of Plant Physiologists


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