- Volume 33 Issue 1
The chloroplast has been the prime light-energy harvesting organelle on earth. It also carries out several key metabolic processes, such as lipid synthesis and nitrogen metabolism. Even though the chloroplast has its own genome, its coding capacity can afford only dozens of proteins, and most of the proteins functioning in the chloroplast are imported from the cytosol where nuclear encoded chloroplast genes are synthesized on free cytosokic ribosomes. Precursor proteins synthesized on cytosolic ribosomes have transit peptides at the amino termini of the proteins, and the transit peptide is sufficient to transfer chloroplast proteins from the cytosol into the chloroplast. When comparing amino acid sequences duduced from the nucleotide sequences of the clones of the chloroplast proteins, high homologies can be found among the transit peptides of proteins with the same function. Overall amino acid compositions of the transit peptides show amphiphilic characters of the transit peptides, and the amphiphilicity indicates that three dimensional structure of the transit peptide is responsible for the translocation of the chloroplast proteins.