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A dinucleotide mutation in dihydrodipicolinate synthase of Nicotiana sylvestris leads to lysine overproduction by Marc Ghislain; Valerie Frankard; Michel Jacobs is a scholarly article available to read on EtoBox.

What is A dinucleotide mutation in dihydrodipicolinate synthase of Nicotiana sylvestris leads to lysine overproduction about?

By applying a mutagenesis/selection procedure to obtain resistance to a lysine analog, __S__‐(2‐aminoethyl)l‐cysteine (AEC), a lysine overproducing mutant in __Nicotiana sylvestris__ was isolated. Amino acid analyses performed throughout plant development and of different organs of the __N. sylvestris__ RAEC‐1 mutant, revealed a developmental‐dependent accumulation of free lysine. Lysine biosynthesis in the RAEC‐1 mutant was enhanced due to a lysine feedback‐desensitized dihydrodipicolinate synthase (DHDPS). Several molecular approaches were undertaken to identify the nucleotide change in the __dhdps‐r1__ gene, the mutated gene coding for the lysine‐desensitized enzyme. The enzyme was purified from wild‐type plants for amino end microsequencing and 10 amino acids were identified. Using dicotyledon __dhdps__ probes, a genomic fragment was cloned from an enriched library of DNA from the homozygote RAEC‐1 mutant plant. A __dhdps__ cDNA, putatively full‐length, was isolated from a tobacco cDNA library. Nucleotide sequence analyses confirmed the presence of the previously identified amino end preceded by a chloroplast transit peptide sequence. Nucleotide sequence comparisons, enzymatic

Author

Marc Ghislain; Valerie Frankard; Michel Jacobs

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0960-7412)

Published

1995

Language

EN