The 49 K subunit of NADH: ubiquinone reductase (complex I) fromNeurospora crassa mitochondria: primary structure of the gene and the protein
✍ Scribed by D. Preis; J. C. Pas; U. Nehls; D. -A. Röhlen; U. Sackmann; U. Jahnke; H. Weiss
- Book ID
- 104721672
- Publisher
- Springer-Verlag
- Year
- 1990
- Tongue
- English
- Weight
- 601 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0172-8083
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✦ Synopsis
The primary structure of the 49 K subunit of the respiratory chain NADH:ubiquinone reductase (complex I) from Neurospora crassa was determined by sequencing cDNA, genomic DNA and the N-terminus of the mature protein. The sequence lengths correlate to a molecular mass of 54,002 daltons for the preprotein and 49,239 daltons for the mature protein. The presequence consists of 42 amino acids of typical composition for sequences which target nuclear-encoded proteins into mitochondria. The mature protein consists of 436 amino acids and shows 64% similarity to a 49 K subunit of bovine heart NADH:ubiquinone reductase and 33% to a predicted translation product of an open reading frame in the chloroplast DNAs of Marchantia polymorpha and Nicotiana tabacum. Evidence for an iron-sulfur cluster in the subunit is discussed.
📜 SIMILAR VOLUMES
Sequence analysis of a transcribed region of mitochondrial DNA (mtDNA) from male fertile sugarbeet (Beta vulgaris L.) revealed an open reading frame showing extensive sequence homology to the subunit 2 gene of the NADH: ubiquinone reductase complex (nad2). Sugarbeet nad2 in common with its proposed