Synthesis of subunit III of CF0 by thylakoid-bound polysomes from pea chloroplasts

Abstract
Wahsed thylakoid membranes from pea chloroplasts incorporate label from (35S)-methionine into protein when supplemented with S-30 soluble factors from E. coli. One of the products associated with the thylakoids is soluble in butanol, precipitated by ether and has an apparent molecular mss of 8200D on urea-lithium dodecyl sulphate (LDS) polyacrylamide gels. In addition, the protein covalently binds dicyclohexylcarbo-diimide (DCCD) which causes it to migrate as two slower forms on gels. Based on these criteria we establish that the proteolipid or subunit III of CF0 (the intrinsic sector of the ATPase complex) is synthesized by the thylakoid bound polysomes.