Mitochondrial Translation

The macroscopic rates measured by radiolabel experiments should not be taken to reflect maximum rates of the motors involved. As with mitochondrial transport, the net rate of slow component proteins reflects both the rate of actual movement and the fraction of a time interval that a structure is moving. The elongate shape of cytoskeletal structures and their potential for many interactions means that net displacements are discontinuous. If a structure is moving at a speed of 2 j,m/s, but on average only moves at that rate for one second out of every 100 seconds, then the average rate for the structure will translate to a net rate of only 0.02 pm/s [31]. 

Mitochondrial DNA is inherited maternally. What makes mitochondrial diseases particularly interesting from a genetic point of view is that the mitochondrion has its own DNA (mtDNA) and its own transcription and translation processes. The mtDNA encodes only 13 polypeptides nuclear DNA (nDNA) controls the synthesis of 90-95% of all mitochondrial proteins. All known mito-chondrially encoded polypeptides are located in the inner mitochondrial membrane as subunits of the respiratory chain complexes (Fig. 42-3), including seven subunits of complex I the apoprotein of cytochrome b the three larger subunits of cytochrome c oxidase, also termed complex IV and two subunits of ATPase, also termed complex V. 

Mitochondrial proteins encoded by nuclear genes are translated by ribosomes free in the cytoplasm, then folded and transferred into the mitochondria by different molecular chaperones. 

An extremely important role of iron is the synthesis of haem for formation of erythrocytes and also for proliferating cells for synthesis of the mitochondrial enzymes that contain haem (e.g. cytochromes). The flux-generating enzyme in the synthesis of haem is aminolevulinic acid synthase (ALS) (Figure 15.20). If the cellular iron concentration is low, the concentration of this enzyme is increased in an attempt to maintain the rate of synthesis. As with the other two proteins, the concentration of ALS is controlled at the level of translation in a similar manner to that for transferrin, i.e. by increased stability of the mRNA, which is achieved by the binding of the IRP to the mRNA. 

The thyroid hormone thyroxine (tetraiodo-thyronine, T4) and its active form triiodothyronine (T3) are derived from the amino acid tyrosine. The iodine atoms at positions 3 and 5 of the two phenol rings are characteristic of them. Post-translational synthesis of thyroxine takes place in the thyroid gland from tyrosine residues of the protein thyro-globulin, from which it is proteolytically cleaved before being released, iodothyronines are the only organic molecules in the animal organism that contain iodine. They increase the basal metabolic rate, partly by regulating mitochondrial ATP synthesis, in addition, they promote embryonic development. 

Biomarkers Translational safety biomarkers (e.g., mitochondrial toxicity can be detected in vitro and in vivo), phospholipidosis [37]... 

Some Mitochondrial Proteins Are Transported after Translation... 

The genetic code differs very little between species. By contrast, considerable differences occur between species in the anticodon translation system of tRNA, as evidenced by the mitochondrial tRNA system. In all systems the bases in the anticodon-codon complex run antiparallel, as in standard double-helix pairing, and in all cases only Watson-Cricklike base pairing occurs between the first two bases in the codon and the opposing bases in the anticodon segment of the tRNA. However, for the 3 base in the codon, the rules for pairing vary with the species and with the base in question. These rules, summarized in table 29.4, are as follows. 

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