E. Glaser et al., MITOCHONDRIAL PROTEIN IMPORT IN PLANTS - SIGNALS, SORTING TARGETING, PROCESSING AND REGULATION, Plant molecular biology, 38(1-2), 1998, pp. 311-338
Mitochondrial biogenesis requires a coordinated expression of both the
nuclear and the organellar genomes and specific intracellular protein
trafficking, processing and assembly machinery. Most mitochondrial pr
oteins are synthesised as precursor proteins containing an N-terminal
extension which functions as a targeting signal, which is proteolytica
lly cleaved off after import into mitochondria. We review our present
knowledge on components and mechanisms involved in the mitochondrial p
rotein import process in plants. This encompasses properties of target
ing peptides, sorting of precursor proteins between mitochondria and c
hloroplasts, signal recognition, mechanism of translocation across the
mitochondrial membranes and the role of cytosolic and organellar mole
cular chaperones in this process. The mitochondrial protein processing
in plants is catalysed by the mitochondrial processing peptidase (MPP
), which in contrast to other sources, is integrated into the bc(1) co
mplex of the respiratory chain. This is the most studied component of
the plant import machinery characterised to date. What are the biochem
ical consequences of the integration of the MPP into an oligomeric pro
tein complex and how are several hundred presequences of precursor pro
teins with no sequence similarities and no consensus for cleavage, spe
cifically cleaved off by MPP? Finally we will address the emerging are
a of the control of protein import into mitochondria.