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A 15 kDa proteolipid found in mediatophore preparations from Torpedo electric organ presents high sequence homology with the bovine chromaffin granule protonophore
Author(s) -
Birman Serge,
Meunier François-Marie,
Lesbats Bernard,
Le Caer Jean-Pierre,
Rossier Jean,
Israël Maurice
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80577-6
Subject(s) - microbiology and biotechnology , biology , torpedo , biochemistry , peptide sequence , homology (biology) , signal peptide , amino acid , gene , acetylcholine receptor , receptor
Upon SDS PAGE of isolated mediatophore, an acetylcholine‐translocating protein, a doublet at 15 kDa was identified. Amino acid sequencing after CNBr cleavage gave a 17 residue‐long peptide completely homologous with a sequence of the proton‐translocating proteolipid from bovine chromaffin granules. A 51‐mer oligodeoxynucleotide corresponding to this sequence was used to screen a library of electric lobe cDNAs constructed in λZap II. A positive recombinant clone was isolated and found to encode the complete sequence of a 15.5 kDa protein highly homologous to the bovine chromaffin or yeast vacuolar ATPase proteolipid. In vitro translation of sense RNA transcripts of the clone indeed yielded a single 15 kDa proteolipid. Northern blot analysis showed that the 1.3 kb mRNA encoding this protein is significantly expressed in nervous tissues but not in electric organ or liver of Torpedo marmorata .