The identity and scope of chloroplast and mitochondrial proteases in higher
plants has only started to become apparent in recent years. Biochemical an
d molecular studies suggested the existence of Clp, FtsH, and DegP protease
s in chloroplasts, and a Lon protease in mitochondria, although currently t
he 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 loca
tion and putative processing sites, and to propose a standard nomenclature
to avoid confusion and facilitate scientific communication. For the Clp pro
tease most of the ClpP isomers are found in chloroplasts, whereas one is mi
tochondrial. Of the ATPase subunits, the one ClpD and two ClpC isomers are
Located in chloroplasts, whereas both ClpX isomers are present in mitochond
ria. Isomers of the Lon protease are predicted in both compartments, as are
the different forms of FtsH protease. DegP, the least characterized protea
se in plant cells, has the most number of isomers and they are predicted to
localize in several cell compartments. These predictions, along with the p
roposed nomenclature, will serve as a framework for future studies of all f
our families of proteases and their individual isomers.