Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits

Abstract

The ribulose-bisphosphate carboxylase large-subunit binding protein from Pisum sativum chloroplasts is an oligomer of two types of subunit with the composition .alpha.6.beta.6. These two subunits are immunologically distinct, show different partial protease digestion patterns and have different amino-terminal sequences. Leaves of Hordeum vulgare also contain an oligomeric binding protein composed of equal amounts of two types of subunit. Treatment of either P. sativum stromal extracts or purified binding protein with ATP and Mg2+ ions causes the dissociation of the oligomeric form of the binding protein to the monomeric subunits. This effet is highly specific for ATP since CTP, UTP, GTP, ADP, AMP, cyclic AMP, NADPH and pyrophosphate do not cause dissociation.