title: A new metallothionein gene from the giant keyhole limpet Megathura crenulata.
abstract: Metallothioneins (MTs) are small soluble proteins ubiquitously expressed in animals and plants. Different isoforms are present in deuterostomes and protostomes. They do not differ greatly in primary structure, but are clearly distinguishable. Here, I present the gene and the complete cDNA of a novel MT from the mollusk Megathura crenulata. This protein is closely related to the Cu-inducible MTs of the vineyard snail Helix pomatia, but has also some minor sequence features typical of Cd-inducible isoforms of H. pomatia and other molluscs. Overall, the deduced primary structure is similar to the known molluscan MTs, but in addition possesses an insertion of 5 amino acids not found in any other molluscan MTs, protostomic or deuterostomic MTs. In addition, a pentapeptide insertion, characteristic of mammalian MT-3 is present but it lacks the functional tetrapeptide CPCP within the beta-region of those MT-3 proteins that are known to suppress neuronal growth processes. The M. crenulata MT is a novel form of MT in comparison to all other known MTs. Possible functional aspects for this new MT are discussed.
authors.affiliation: Institute of Zoology, Johannes Gutenberg University of Mainz, D-55099 Mainz, Germany. lieb@mail.uni-mainz.de
authors.forename: Bernhard
authors.initials: B
authors.lastname: Lieb
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000032:analysis; D018076:DNA, Complementary / Q000235:genetics; D016678:Genome; D008668:Metallothionein / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D008974:Mollusca / Q000235:genetics*; D016133:Polymerase Chain Reaction; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
chemical_list: D002352:Carrier Proteins; D018076:DNA, Complementary; C023548:copper-binding protein; D008668:Metallothionein