Towards a comparative anatomy of N-terminal topogenic protein sequences.
A comparative study of three kinds of eukaryotic N-terminal topogenic sequences, viz signal peptides, N-terminal transmembrane anchors, and mitochondrial targeting sequences, suggests: that the sign of the N-terminal charge might influence the orientation of an N-terminal hydrophobic segment relative to the membrane and give rise to N-terminally anchored proteins with their main mass exposed either on the cytosolic or extra-cytosolic side of the membrane; and that N-terminal transmembrane segments in mitochondrial targeting sequences have a relatively low overall hydrophobicity, probably in order to avoid being recognized by the endoplasmic reticulum export machinery.
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D002736:Chloroplasts / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D008954:Models, Biological; D021382:Protein Sorting Signals / Q000378:metabolism*; D051381:Rats; D013816:Thermodynamics
D008565:Membrane Proteins; D021382:Protein Sorting Signals