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Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding nitrate reductase, a metalloflavoprotein with three functional domains

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
; ; ;  [1]
  1. Stanford Univ. School of Medicine, CA (USA)
The sequence of nitrate reductase mRNA from the plant Arabidopsis thaliana has been determined. A 3.0-kilobase-long cDNA was isolated from a {lambda}gt10 cDNA library of Arabidopsis leaf poly(A){sup +} RNA. The cDNA hybridized to a 3.2-kilobase mRNA whose level increased 15-fold in response to treatment of the plant with nitrate. An open reading frame encoding a 917 amino acid protein was found in the sequence. This protein is very similar to tobacco nitrate reductase, being >80% identical within a section of 450 amino acids. By comparing the Arabidopsis protein sequence with other protein sequences, three functional domains were deduced: (i) a molybdenum-pterin-binding domain that is similar to the molybdenum-pterin-binding domain of rat liver sulfite oxidase, (ii) a heme-binding domain that is similar to proteins in the cytochrome b{sub 5} superfamily, and (iii) an FAD-binding domain that is similar to NADH-cytochrome b{sub 5} reductase.
DOE Contract Number:
FG03-84ER13265
OSTI ID:
5365126
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 85:14; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English

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