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Characterization of a cDNA clone encoding the complete amino acid sequence of cotton isocitrate lyase
R B Turley1, S M Choe, R N Trelease
1Department of Botany, Arizona State University, Tempe 85287-1601.
Biochimica Et Biophysica Acta
|June 21, 1990
Abstract:
A cDNA clone encoding the glyoxysomal enzyme isocitrate lyase (ICL) (EC 4.1.3.1) was isolated from a library prepared from cotton (Gossypium hirsutum L.) cotyledon poly(A)+ RNA. The clone is 1893 basepairs (bp) in length and contains a 1728 bp open reading frame encoding a polypeptide of 576 residues (Mr = 64,741). The deduced amino acid sequence of cotton ICL is 85.2%, 90.3% and 41.1% identical to ICL from rapeseed, castor bean and E. coli, respectively. Cotton ICL has a C-terminal tripeptide of A-R-M which is a putative trafficking signal for peroxisome (glyoxysome) proteins.