Eur J Biochem 1983 Oct 17;1361:141-6.

Signal sequences, secondary modification and the turnover of miscompartmentalized secretory proteins in Xenopus oocytes.

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The cytoplasm of the Xenopus oocyte can be altered by the microinjection of proteins and the regulatory responses to such perturbations can then be studied. We have investigated proteolytic systems within the oocyte which may be involved in the maintenance of the integrity of the different subcellular compartments. Thus primary translation products, made in the wheat germ system under the direction of frog liver, chicken oviduct, rat liver rapidly sedimenting endoplasmic reticulum, rat seminal vesicle, guinea pig mammary gland or honey been venom gland RNA, were injected into oocytes. Their stability in the frog cell cytosol was in general low compared to that of their processed counterparts. The latter were usually obtained by collecting the heterologous proteins exported by RNA-injected oocytes. Electrophoretic analysis of oocytes injected with particular primary and processed polypeptides permitted measurement of the stabilities of proteins differing only by the presence or absence of a detachable signal sequence, or by the presence of a specific secondary modification. The effect of the latter on protein stability appears slight. However, the presence of a detachable signal sequence destabilizes those miscompartmentalized secretory proteins which are otherwise stable. Indeed all other results are consistent with this concept for they show that primary translation products are in general much less and are never more stable than their processed counterparts. Thus we provide evidence that errors of compartmentation can be corrected in living cells and that this process is often facilitated by the properties conferred on a protein by a detachable signal sequence.

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