Primary structure, in vitro expression and import into mitochondria of a 29/21-kDa subunit of complex I from Neurospora crassa.
A full-length cDNA clone coding for a cytoplasmically-synthesized subunit of complex I from Neurospora crassa (apparent molecular mass of 29 kDa) was isolated. DNA sequencing revealed an open reading frame coding for a protein containing 201 amino acids. A molecular mass of 21323 Da was calculated. The precursor polypeptide was efficiently expressed in vitro and imported into isolated mitochondria. It is synthesized without a cleavable signal sequence and needs a membrane potential in order to bind to the mitochondrial membranes.
Videira
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A
Institut für Physiologische Chemie der Universität München, Federal Republic of Germany.
Tropschug
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M
Werner
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S
D000595:Amino Acid Sequence; D001483:Base Sequence; D015870:Gene Expression; D005800:Genes, Fungal; D005822:Genetic Vectors; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016660:NAD(P)H Dehydrogenase (Quinone); D009491:Neurospora / Q000235:genetics*; D009492:Neurospora crassa / Q000201:enzymology / Q000235:genetics*; D011487:Protein Conformation; D011808:Quinone Reductases / Q000235:genetics* / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D015183:Restriction Mapping
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D016660:NAD(P)H Dehydrogenase (Quinone); D011808:Quinone Reductases