Fructose 1,6-bisphosphate aldolase activity in leaves of a rice mutant selected for enhanced lysine.
Unknown proteins isolated from mutant tissues of rice (Oryza sativa L.) recovered from inhibitor selections were subsequently peptide microsequenced. Database searches putatively identified one peptide as fructose 1,6-bisphosphate aldolase (EC 4.1.2.13). Tissues of mutant rice, PI564784, and wild type (cv Calrose 76) tissues were evaluated for aldolase activity. Total enzyme activities were slightly lower in the mutant than the control but the differences were not significant. Although the mutant phenotype is for enhanced lysine and protein, we ascribe the small aldolase differences to physiological adjustments, rather than to DNA modifications of the aldolase gene(s). Homologies of rice peptides with aldolases from a range of species, as well as rice cell culture expressed sequence tags (ESTs) are presented. Some amino acids sequences are highly conserved. The mutant phenotype expressing stress proteins is not likely to be defined by a change in rice aldolases.
Schaeffer
G W
GW
USDA, ARS, Plant Sciences Institute, Beltsville, Md. 20705, USA.
Sharpe
F T
FT
Sicher
R C
RC
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D012275:Oryza / Q000201:enzymology* / Q000235:genetics; D018515:Plant Leaves / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid
D005634:Fructose-Bisphosphate Aldolase; D008239:Lysine