{PDOC00299} {PS00342; MICROBODIES_CTER} {BEGIN} ******************************************* * Microbodies C-terminal targeting signal * ******************************************* Microbodies are a class of small, single membraned organelles to which belong peroxisomes, glyoxysomes, and glycosomes. Microbody proteins are synthesized on free polysomes and imported into the organelle post-translationally. Unlike the import of proteins into mitochondria, chloroplasts or the ER/secretion pathway, import into microbodies does not generally require the removal of a presequence [1]. It has been experimentally shown [2,3,4] that, in some peroxisomal proteins, the targeting signal (PTS) resides in the last three amino acids of the C-terminus. This consensus sequence is known as 'S-K-L' (Ser-Lys-Leu), although some variations are allowed in all three positions. As the peroxisomal targeting signal also seems to be recognized by other microbodies, it is now [1] known as the C-terminal microbody targeting signal (CMTS). It must be noted that not all microbody proteins contain a CMTS; some seem to contain an internal CMTS-like sequence, but it is not yet known if it is active as such. Finally, a few proteins are synthesized with an N-terminal presequence which is cleaved off during import. Microbody proteins known or thought to contain a CMTS are listed below. - Mammalian D-amino acid oxidase. - Mammalian acyl-coenzyme A oxidase (but not the fungal enzymes). - Mammalian and yeast (S. cerevisiae) carnitine o-acetyltransferase. - Mammalian trifunctional fatty acid beta oxidation pathway enzyme. - Mammalian, insect, plants, and Aspergillus uricase. - Mammalian sterol carrier protein-2 high molecular form (SCP-X). - Mammalian long chain alpha-hydroxy acid oxidase. - Mammalian soluble epoxide hydrolase (sEH). - Firefly luciferase. - Plants glycolate oxidase. - Plants glyoxisomal isocitrate lyase. - Plants and fungal glyoxisomal malate synthase. - Trypanosoma glycosomal glucose-6-phosphate isomerase. - Trypanosoma glycosomal glyceraldehyde 3-phosphate dehydrogenase. - Yeast (H. polymorpha and Pichia pastoris) alcohol oxidase (AOX). - Yeast (H. polymorpha) dihydroxy-acetone synthase (DHAS). - Yeast (S. cerevisiae) catalase A. - Yeast (S. cerevisiae) citrate synthase. - Yeast (S. cerevisiae) peroxisomal malate dehydrogenase. - Yeast (C. boidinii) peroxisomal protein PMP20. - Yeast (C. tropicalis) hydratase-dehydrogenase-epimerase (HDE) from fatty acid beta oxidation pathway. - Yeast (C. tropicalis) isocitrate lyase. - Aspergillus niger monoamine oxidase N. - Candida albicans vacuolar aspartic protease PRA1. -Consensus pattern: [STAGCN]-[RKH]-[LIVMAFY]> -Last update: November 1997 / Pattern and text revised. [ 1] De Hoop M.J., Ab G. Biochem. J. 286:657-669(1992). [ 2] Gould S.J., Keller G.-A., Subramani S. "Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins." J. Cell Biol. 107:897-905(1988). PubMed=2901422 [ 3] Gould S.J., Keller G.-A., Hosken N., Wilkinson J., Subramani S. "A conserved tripeptide sorts proteins to peroxisomes." J. Cell Biol. 108:1657-1664(1989). PubMed=2654139 [ 4] Gould S.J., Keller G.-A., Schneider M., Howell S.H., Garrard L.J., Goodman J.M., Distel B., Tabak H., Subramani S. "Peroxisomal protein import is conserved between yeast, plants, insects and mammals." EMBO J. 9:85-90(1990). PubMed=2104803 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}