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Targeting of Proteins to Mitochondria and Chloroplasts
Most mitochondrial and chloroplast proteins are encoded by nuclear genes, synthesized on cytosolic ribosomes, and imported post-
All the information required to target a precursor protein from the cytosol to the mitochondrial matrix or chloroplast stroma is contained within its N-
Cytosolic chaperones maintain the precursors of mitochondrial and chloroplast proteins in an unfolded state. Only unfolded proteins can be imported into the organelles. Translocation in mitochondria occurs at sites where the outer and inner membranes of the organelles are close together.
Proteins destined for the mitochondrial matrix bind to receptors on the outer mitochondrial membrane and are then transferred to the general import pore (Tom40) in the outer membrane. Translocation through the outer and inner membranes occurs concurrently. Translocation is driven by ATP hydrolysis by Hsp70 in the matrix (see Figure 13-24) and by the proton-
Proteins sorted to mitochondrial destinations other than the matrix usually contain two or more targeting sequences, one of which may be an N-
Some mitochondrial proteins destined for the intermembrane space or inner membrane are first imported into the matrix and then redirected; others never enter the matrix, but go directly to their final location.
Protein import into the chloroplast stroma occurs through outer-
Proteins destined for the thylakoid have secondary targeting sequences. After entry of these proteins into the stroma, cleavage of the stromal-
The four known pathways for moving proteins from the chloroplast stroma to the thylakoid closely resemble translocation across the bacterial plasma membrane (see Figure 13-29). One of these systems can translocate folded proteins.