Plant aldolase: cDNA and deduced amino-acid sequences of the chloroplast and cytosol enzyme from spinach |
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Authors: | Birgit Pelzer-Reith Anja Penger Claus Schnarrenberger |
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Affiliation: | (1) Institut für Pflanzenphysiologie und Mikrobiologie, Freie Universität Berlin, Königin-Luise-Strasse 12-16a, D-1000 Berlin 33, Germany |
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Abstract: | We report the sequences of full-length cDNAs for the nuclear genes encoding the chloroplastic and cytosolic fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) from spinach. A comparison of the deduced amino-acid sequences with one another and with published cytosolic aldolase sequences of other plants revealed that the two enzymes from spinach share only 54% homology on their amino acid level whereas the homology of the cytosolic enzyme of spinach with the known sequences of cytosolic aldolases of maize, rice and Arabidopsis range from 67 to 92%. The sequence of the chloroplastic enzyme includes a stroma-targeting N-terminal transit peptide of 46 amino acid residues for import into the chloroplast. The transit peptide exhibits essential features similar to other chloroplast transit peptides. Southern blot analysis implies that both spinach enzymes are encoded by single genes. |
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Keywords: | cDNA sequences evolution fructose-1,6-bisphosphate aldolase Spinacia oleracea transit peptide |
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