title: Cloning of sponge (Geodia cydonium) and tunicate (Botryllus schlosseri) proteasome subunit epsilon (PRCE): implications about the vertebrate MHC-encoded homologue LMP7 (PRCC).
abstract: Proteasomes are large protein complexes that play a major role in selective degradation of intracellular proteins. Eukaryotes feature seven different alpha and beta subunits. Two of the vertebrate housekeeping beta-subunits have MHC-encoded homologues that can substitute for the housekeeping counterparts upon interferon-gamma induction. In the present study we report the cloning of invertebrate beta-subunit proteasome epsilon (PRCE), from the marine sponge Geodia cydonium and from the colonial tunicate Botryllus schlosseri. Sequence comparisons revealed that the sponge and tunicate proteins are strikingly similar to vertebrate and yeast PRCEs and their MHC-linked counterparts the PRCCs (also termed LMP7), and to a lesser degree also to archaebacterial proteasome subunit beta. Based on this comparison we suggest that all eukaryotic PRCEs and PRCCs feature a cleavable N-terminal propeptide, including the two mammalian PRCEs which appear to have been wrongly predicted from incomplete cDNAs. Our comparative analysis outlines 25 amino acid positions which appear to be unique for PRCCs, distinct from the corresponding residues in metazoan PRCEs.
authors.affiliation: Institut für Physiologische Chemie, Abteilung Angewandte Molekularbiologie, Universität, Mainz, Germany.
authors.forename: Z
authors.initials: Z
authors.lastname: Pancer
authors.forename: U
authors.initials: U
authors.lastname: Scheffer
authors.forename: I
authors.initials: I
authors.lastname: Müller
authors.forename: W E
authors.initials: WE
authors.lastname: Müller
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002645:Chickens; D003001:Cloning, Molecular; D016384:Consensus Sequence; D003546:Cysteine Endopeptidases / Q000096:biosynthesis* / Q000737:chemistry*; D017931:DNA Primers; D018076:DNA, Complementary; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000096:biosynthesis* / Q000737:chemistry*; D010802:Phylogeny; D016133:Polymerase Chain Reaction; D011161:Porifera / Q000201:enzymology*; D046988:Proteasome Endopeptidase Complex; D011506:Proteins / Q000737:chemistry*; D051381:Rats; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D014561:Urochordata / Q000201:enzymology*; D014714:Vertebrates
chemical_list: D017931:DNA Primers; D018076:DNA, Complementary; D009097:Multienzyme Complexes; D011506:Proteins; D003546:Cysteine Endopeptidases; C077436:LMP7 protein; D046988:Proteasome Endopeptidase Complex; C102382:proteasome subunit epsilon, Botryllus; C102381:proteasome subunit epsilon, Geodia