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ATP‐released large subunits participate in the assembly of RuBP carboxylase
Author(s) -
Milos Patrice,
Roy Harry
Publication year - 1984
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240240206
Subject(s) - protein subunit , chemistry , biochemistry , dissociation (chemistry) , chloroplast , nucleotide , methionine , biophysics , biology , amino acid , gene
Preincubation of 35 S‐methionine‐labeled chloroplast extracts with ATP at 0°C potentiates the subsequent assembly of labeled large subunits into RuBPCase. This is correlated with the dissociation of newly synthesized large subunits from the 29S large subunit binding protein complex. These released large subunits then assemble into RuBPCase in a second, nucleotide‐stimulated reaction. The data demonstrate that the 29S complex can play an active role in the assembly of RuBPCase.