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

Nora Plesofsky, Nancy Gardner, Arnaldo Videira, Robert Brambl

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


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 [3H]myristic acid was incorporated by Neurospora crassa into the mitochondrial-encoded, ~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. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)223-230
Number of pages8
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number3
StatePublished - Feb 28 2000

Bibliographical note

Funding Information:
This research was supported by the National Institute of General Medical Sciences (GM-19398) and the National Research Initiative of the USDA Competitive Research Grants Office (94-37100-0290).


  • Mitochondria
  • Myristoylation
  • NADH dehydrogenase
  • Neurospora crassa


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