A NOVEL SIGNAL RECOGNITION PARTICLE TARGETS LIGHT-HARVESTING PROTEINSTO THE THYLAKOID MEMBRANES

The mechanisms involved in the posttranslational targeting of membrane proteins are not well understood. The light-harvesting chlorophyll pr oteins (LHCP) of the thylakoid membrane are a large family of hydropho bic proteins that are targeted in this manner. They are synthesized in the cytoplasm, translocated across the chloroplast envelope membranes into the stroma, bound by a stromal factor to form a soluble intermed iate, ''transit complex'', and then integrated into the thylakoid memb rane by a GTP dependent reaction. Signal recognition particle (SRP), a cytoplasmic ribonucleoprotein, is known to mediate the GTP dependent cotranslational targeting of proteins to the endoplasmic reticulum. We show that chloroplasts contain an SRP consisting of, cpSRP54, a homol ogue of SRP54 and a previously undescribed 43-kDa polypeptide (cpSRP43 ) instead of an RNA. We demonstrate that both subunits of cpSRP are re quired for the formation of the transit complex with LHCP. Furthermore , cpSRP54, cpSRP43, and LHCP are sufficient to form a complex that app ears to be identical to authentic transit complex. We also show that t he complex formed between LHCP and cpSRP, together with an additional soluble factor(s) are required for the proper integration of LHCP into the thylakoid membrane. It appears that the expanded role of cpSRP in posttranslational targeting of LHCP has arisen through the evolution of the 43-kDa protein.