How signal sequences maintain cleavage specificity.
The specificity of the signal sequence cleavage reaction has been postulated to reside in a signal peptidase active site that can bind only to particular (i, i + 2) pairs of amino acids. In this paper, we present further patterns of non-random amino acid utilization in a region around in vivo cleavage sites, and show that they can be interpreted in terms of selection acting to reduce the number of potential competing sites in the vicinity of the correct one.
D000409:Alanine / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D010450:Endopeptidases / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000378:metabolism; D005998:Glycine / Q000378:metabolism; D008565:Membrane Proteins; D010455:Peptides / Q000378:metabolism*; D011387:Prokaryotic Cells / Q000378:metabolism; D021382:Protein Sorting Signals; D012694:Serine / Q000378:metabolism; D012697:Serine Endopeptidases
D008565:Membrane Proteins; D010455:Peptides; D021382:Protein Sorting Signals; D012694:Serine; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase; D000409:Alanine; D005998:Glycine