Open AccessPatterns of Amino Acids near Signal‐Sequence Cleavage Sites
Author(s) -
HEIJNE Gunnar
Publication year - 1983
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1983.tb07424.x
Subject(s) - cleavage (geology) , signal peptide , signal peptidase , endoplasmic reticulum , protein sorting signals , amino acid , sequence (biology) , signal (programming language) , cleavage factor , protein sequencing , peptide sequence , chemistry , biology , biochemistry , computer science , paleontology , rna , fracture (geology) , gene , programming language
According to the signal hypothesis, a signal sequence, once having initiated export of a growing protein chain across the rough endoplasmic reticulum, is cleaved from the mature protein at a specific site. It has long been known that some part of the cleavage specificity resides in the last residue of the signal sequence, which invariably is one with a small, uncharged side‐chain, but no further specific patterns of amino acids near the point of cleavage have been discovered so far. In this paper, some such patterns, based on a sample of 78 eukaryotic signal sequences, are presented and discussed, and a first attempt at formulating rules for the prediction of cleavage sites is made.