Mitochondrial ribosomal proteins (MRPs) are the counterparts in that o
rganelle of the cytoplasmic ribosomal proteins in the host. Although t
he MRPs fulfil similar functions in protein biosynthesis, they are dis
tinct in number, features and primary structures from the latter. Most
progress in the eludication of the properties of individual MRPs, and
in the characterization of the corresponding genes, has been made in
baker's yeast (Saccharomyces cerevisiae). To date, 50 different MRPs h
ave been determined, although biochemical data and mutational analysis
propose a total number which is substantially higher. Surprisingly, o
nly a minority of the MRPs that have been characterized show significa
nt sequence similarities to known ribosomal proteins from other source
s, thus limiting the deduction of their functions by simple comparison
of amino acid sequences. Further, individual MRPs have been character
ized functionally by mutational studies, and the regulation of express
ion of MRP genes has been described. The interaction of the mitochondr
ial ribosomes with transcription factors specific for individual mitoc
hondrial mRNAs, and the communication between mitochondria and the nuc
leus for the co-ordinated expression of ribosomal constituents, are ot
her aspects of current MRP research. Although the mitochondrial transl
ational system is still far from being described completely, the yeast
MRP system serves as a model for other organisms, including that of h
umans.