The mitochondrial targeting signal also known as presequence is a 10-70 amino acid long peptide that directs a newly synthesized protein to the mitochondria. It is found at the N-terminus end consists of an alternating pattern of hydrophobic and positively charged amino acids to form what is called an amphipathic helix. Mitochondrial targeting signals can contain additional signals that subsequently target the protein to different regions of the mitochondria, such as the mitochondrial matrix or inner membrane. In plants, an N-terminal signal (or transit peptide) targets to the plastid in a similar manner. Like most signal peptides, mitochondrial targeting signals and plastid specific transit peptides are cleaved once targeting is complete. Some plant proteins have an N-terminal transport signal that targets both organelles often referred to as dual-targeted transit peptide. Approximately 5% of total organelle proteins are predicted to be dual-targeted however the specific number could be higher considering the variable degree of accumulation of passenger proteins in both organelles. The targeting specificity of these transit peptides depends on many factors including net charge and affinity between transit peptides and organelle transport machinery.