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J. Biol. Chem., Vol. 265, Issue 2, 808-814, Jan, 1990
GS Hudson, JD Mahon, PA Anderson, MJ Gibbs, MR Badger, TJ Andrews and PR Whitfeld
Ribulosebisphosphate carboxylase/oxygenase from C4 plants exhibits higher
turnover rates and lower affinities for CO2 than the enzyme from C3 plants
or C3-C4 intermediate species. This property is shown to be inherited
maternally in reciprocal interspecific crosses between two Flaveria
species, and thus must be specified by the chloroplast-encoded large
subunits. To investigate the amino acid changes responsible, the
chloroplast rbcL genes from three pairs of C3 and C4 species from three
genera (Flaveria, Atriplex, and Neurachne) were cloned and sequenced.
Comparisons of the predicted amino acid sequences from species of the same
genus revealed a limited number of changes within each pair, ranging from
three to six, of which only one (309Met (C3) to Ile (C4] was consistently
observed. This residue occurs in the loop connecting the carboxyl end of
beta strand 5 with the amino end of alpha helix 5 in the alpha/beta barrel
of the large subunit, and is close to the active site in a region which
makes interdomain and intersubunit contacts. However, it is unlikely that a
change of this residue alone is responsible for the alteration of kinetic
properties. Nucleotide sequence comparisons of the rbcL genes showed no
significant or consistent changes in the promoter and transcribed but
nontranslated regions to suggest why rbcL is not expressed in C4 leaf
mesophyll cells. It is concluded that mutations in rbcL have led to an
alteration of the kinetics but not the expression of ribulose-bisphosphate
carboxylase.
Comparisons of rbcL genes for the large subunit of ribulose- bisphosphate carboxylase from closely related C3 and C4 plant species
Commonwealth Scientific and Industrial Research Organization Division of Plant Industry, Canberra, Australia.
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