NADH dehydrogenase in Neurospora crassa contains myristic acid covalently linked to the ND5 subunit peptide
نویسندگان
چکیده
منابع مشابه
Cytochrome c oxidase in Neurospora crassa contains myristic acid covalently linked to subunit 1.
Radiolabel from [3H]myristic acid was incorporated by Neurospora crassa into the core catalytic subunit 1 of cytochrome c oxidase (EC 1.9.3.1), as indicated by immunoprecipitation. This modification of the subunit, which was specific for myristic acid, represents an uncommon type of myristoylation through an amide linkage at an internal lysine, rather than an N-terminal glycine. The [3H]myrista...
متن کاملThe internal alternative NADH dehydrogenase of Neurospora crassa mitochondria.
An open reading frame homologous with genes of non-proton-pumping NADH dehydrogenases was identified in the genome of Neurospora crassa. The 57 kDa NADH:ubiquinone oxidoreductase acts as internal (alternative) respiratory NADH dehydrogenase (NDI1) in the fungal mitochondria. The precursor polypeptide includes a pre-sequence of 31 amino acids, and the mature enzyme comprises one FAD molecule as ...
متن کاملTight control of respiration by NADH dehydrogenase ND5 subunit gene expression in mouse mitochondria.
A mouse cell variant carrying in heteroplasmic form a nonsense mutation in the mitochondrial DNA-encoded ND5 subunit of the respiratory NADH dehydrogenase has been isolated and characterized. The derivation from this mutant of a large number of cell lines containing between 4 and 100% of the normal number of wild-type ND5 genes has allowed an analysis of the genetic and functional thresholds op...
متن کاملPeptide utilization by nitrogen-starved Neurospora crassa.
Peptides ranging in size from a mean number of 30 residues down to dipeptides supported growth of a leucine auxotroph when used as both a nitrogen and leucine source. Under nitrogen-limiting conditions, the peptides induced extracellular peptidohydrolytic activity, hydrolyzing peptides to monomer amino acids. Growth of a leu-2 mutant of Neurospora crassa on those peptides transportable by the o...
متن کاملThe dihydroxy acid dehydratase of Neurospora crassa.
The dihydroxy acid dehydratase of Neurospora crassa was purified lOOto 150-fold by fractionation with protamine sulfate, ammonium sulfate, Sephadex, and DEAE-Sephadex. It was found that the purified protein migrated in an electric field as a single band on acrylamide gel and in the analytical centrifuge. It had a lipid content of 44 to 50%. The enzyme activity was stabilized by the presence of ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
سال: 2000
ISSN: 0167-4889
DOI: 10.1016/s0167-4889(99)00170-6