NADH dehydrogenase in Neurospora crassa contains myristic acid covalently linked to the ND5 subunit peptide

• Type: Article in International Scientific Journal
• Date: 2000

Authors

plesofsky, n (Author) Other; gardner, n (Author) Other; videira, a (Author) ICBAS; brambl, r (Author) Other

Journal

Title: Biochimica et Biophysica Acta - Molecular Cell Research

Vol. 1495

Pages: 223-230

ISSN: 0167-4889

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 10 Citations

Scopus - 11 Citations

Other information

Authenticus ID: P-001-0SM

DOI: 10.1016/S0167-4889(99)00170-6

Abstract (EN): The mitochondrial, proton-pumping NADH:ubiquinone oxidoreductase consists of at least 35 subunits whose synthesis is divided between the cytosol and mitochondria; this complex I catalyzes the first steps of mitochondrial electron transfer and proton translocation. Radiolabel from [H-3]myristic acid was incorporated by Neurospora crassa into the mitochondrial-encoded, similar to 70 kDa ND5 subunit of NADH dehydrogenase, as shown by immunoprecipitation. This myristate apparently was linked to the peptide through an amide linkage at an invariant lysine residue (Lys546), based upon analyses of proteolysis products, The myristoylated lysine residue occurs in the predicted transmembrane helix 17 (residues 539-563) of ND5. A consensus amino acid sequence around this conserved residue exists in homologous subunits of NADH dehydrogenase. Cytochrome c oxidase subunit 1, in all prokaryotes and eukaryotes, contains this same consensus sequence surrounding the lysine which is myristoylated in N. crassa. (C) 2000 Elsevier Science B.V. All rights reserved.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 8