Genetic and biochemical analysis of intragenic complementation events among nitrate reductase apoenzyme-deficient mutants of Nicotiana plumbaginifolia.

• DOI: 10.1093/genetics/127.1.199
• Publication Date: 2021-01-13T17:36:49Z
• Authors: F Pelsy; M Gonneau
• Keywords: Wild type; Protein-fragment complementation assay

Abstract Intragenic complementation has been observed between apoenzyme nitrate reductase-deficient mutants (nia) of Nicotiana plumbaginifolia. In vivo as in vitro, the NADH-nitrate reductase (NR) activity plants heterozygous for two different nia alleles was lower than wild type plant, but were able to grow on a sole nitrogen source. NR activity, absent extracts homozygous restored by mixing from complementing mutants. These observations suggest that intragenic results either formation heteromeric or interaction modified enzymes. Complementation only retaining partial catalytic activities enzyme. Results are agreement with molecular data suggesting presence three domains subunit