Peptide deformylase

Multicellular living organisms and unmodified parts thereof and – Plant – seedling – plant seed – or plant part – per se

Reexamination Certificate

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Details

C435S006120, C435S069100, C435S468000, C435S419000, C435S252300, C435S320100, C435S183000, C530S370000, C536S023600, C800S278000

Reexamination Certificate

active

07034206

ABSTRACT:
This invention relates to an isolated nucleic acid fragment encoding a metalloprotease, more specifically peptide deformylase. The invention also relates to the construction of a recombinant DNA construct encoding all or a portion of peptide deformylase, in sense or antisense orientation, wherein expression of the recombinant DNA construct results in production of altered levels of peptide deformylase in a transformed host cell.

REFERENCES:
Walbot V. Maize ESTs from various cDNA libraries sequenced at Standford University. EST database, direct submission, Acc No. AI712111, Feb. 2, 2000.
T. Meinnel et. al., BIOCHIMIE, vol. 75:1061-1075, Methionine as Translation Start Signal: A Review of the Enzymes ot the Pathway inEscherichia coli.
Carmela Giglione et. al., The Embo Journal, vol. 19:5916-5929, 2000, Identification of Eukaryotic Peptide Deformylases Reveals Universality of N-Terminal Protein Processing Mechanisms.
National Center for Biotechnology Information General Identifier No. 17433049, Jun. 15, 2002, Giglione, C. et. al., Identification of Eukaryotic Peptide Deformylases Reveals Universality of N-Terminal Protein Processing Mechanisms.
National Center for Biotechnology Information General Identifier No. 15290077, Nov. 29, 2002, Sasaki, T. et. al., The Genome Sequence and Structure of Rice Chromosome 1.
Takuji Sasaki et. al., Nature, vol. 420:312-316, 2002, The Genome Sequence and Structure of Rice Chromosome 1.
Lynnette M.A. Dirket. al., Plant Physiology, vol. 127:97-107, 2001, Eukaryotic Peptide Deformylases. Nuclear-Encoded and Chloroplast-Targeted Enzymes in Arabidopsis.
Thierry Meinnel et. al., Journal of Bacteriology, vol. 177:1883-1887, 1995, Enzymatic Properties ofEscherichia coliPeptide Deformylase.
T. Meinnel et al., J. Mol. Biol., vol. 267:749-761, 1997, Structure-Function Relationships Within the Peptide Deformylase Family. Evidence for a Conserved Architecture of the Active Site Involving Three Conserved Motifs and a Metal Ion.
National Center for Biotechnology Information General Identifier No. 11320967, Nov. 23, 2000, Giglione, C. et. al., Identification of Eukaryotic Peptide Deformylases Reveals Universality of N-Terminal Protein Processing Mechanisms.

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