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J. Biol. Chem., Vol. 262, Issue 32, 15327-15329, 11, 1987
FW Larimer, EH Lee, RJ Mural, TS Soper and FC Hartman
Ribulose bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum is a
homodimer of 50.5-kDa subunits with two substrate binding sites per
molecule of dimer. To determine whether each subunit contains an
independent active site or whether the active sites are created by
intersubunit interactions, we have used a novel in vivo approach for
producing heterodimers from catalytically inactive, site-directed mutants
of the carboxylase. When the alleles encoding these mutant proteins are
placed separately into compatible plasmids and coexpressed in the same
Escherichia coli host, activity is observed at about 20% of the wild-type
level. Analysis of the carboxylase purified from these cells reveals the
presence of heterodimers of the two mutant proteins. This interallelic
complementation demonstrates that domains from each of the subunits
interact to form a shared active site.
Intersubunit location of the active site of ribulose-bisphosphate carboxylase/oxygenase as determined by in vivo hybridization of site- directed mutants [published erratum appears in J Biol Chem 1988 Feb 15;263(5):2575]
Biology Division, Oak Ridge National Laboratory, Tennessee 37831.
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