Towards a comparative anatomy of N-terminal topogenic protein sequences

J Mol Biol. 1986 May 5;189(1):239-42. doi: 10.1016/0022-2836(86)90394-3.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Transport
  • Chloroplasts / metabolism
  • Humans
  • Membrane Proteins / metabolism
  • Mitochondria / metabolism
  • Models, Biological
  • Protein Sorting Signals / metabolism*
  • Rats
  • Thermodynamics

Substances

  • Membrane Proteins
  • Protein Sorting Signals