A 15 kDa proteolipid found in mediatophore preparations from Torpedo electric organ presents high sequence homology with the bovine chromaffin granule protonophore

FEBS Letters

Israël, Maurice²  Birman, Serge²  Lesbats, Bernard²  Rossier, Jean¹  Le Caer, Jean-Pierre¹  Meunier, François-Marie² 

[1] Laboratoire de Physiologie Nerveuse, CNRS, 91198 Gif-sur-Yvette Cedex, France;Laboratoire de Neurobiologie Cellulaire et Moléculaire, Département de Neurochimie, CNRS, 91198 Gif-sur-Yvette Cedex, France

关键词: Mediatophore;    Acetylcholine release;    Proteolipid;    H+-ATPase;    cDNA cloning;    (Torpedo marmorata);   

DOI  :  10.1016/0014-5793(90)80577-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown