Primary structure and expression of a nuclear-coded subunit of complex I homologous to proteins specified by the chloroplast genome.
A 31-kDa subunit of complex I from Neurospora crassa, of nuclear origin, was cloned. The precursor polypeptide (33 kDa) could be efficiently expressed in an in vitro system for transcription and translation. The processing of the precursor to the mature protein was also obtained in vitro. An open reading frame coding for a precursor protein of 283 amino acids (32247 Da) was found by DNA sequencing. The predicted primary structure shows significant homology with proteins made in chloroplast. This supports the hypothesis that an enzyme similar to respiratory chain NADH dehydrogenase might exist in these organelles.
Videira
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Institut für Physiologische chemie, Universität München, Federal Republic of Germany.
Tropschug
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Werner
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D000595:Amino Acid Sequence; D001483:Base Sequence; D002467:Cell Nucleus / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism*; D003001:Cloning, Molecular; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D009245:NADH Dehydrogenase / Q000737:chemistry / Q000235:genetics*; D009492:Neurospora crassa / Q000201:enzymology / Q000235:genetics*; D010940:Plant Proteins / Q000235:genetics*; D010944:Plants / Q000235:genetics* / Q000378:metabolism; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid
D046911:Macromolecular Substances; D010940:Plant Proteins; D009245:NADH Dehydrogenase