Abstract
The calcium pump protein (CPP) or Ca2+-ATPase is the predominant integral membrane protein of the sarcoplasmic reticulum (SR) of skeletal muscle1,2. CPP is a single polypeptide chain of molecular weight (MW) 119,000 (ref. 3) which loops in and out of the membrane at least three times4–8. Recently, a number of integral transmembrane proteins possessing a single hydrophilic domain on each side of the membrane have been observed to use a signal sequence, cleaved9,10 or uncleaved11, to initiate translocation of their ectoplasmic domain12. Microsomal membranes when present during translation are capable of correctly integrating these de novo synthesized proteins into the membrane9,11. We have used this in vitro translocation system to investigate the integration of CPP into the microsomal membrane. We found that CPP is synthesized without a cleaved signal sequence and that it can be integrated into heterologous microsomal membranes only when these are present during translation, but not when they are present after completion of translation.
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Mostov, K., DeFoor, P., Fleischer, S. et al. Co-translational membrane integration of calcium pump protein without signal sequence cleavage. Nature 292, 87–88 (1981). https://doi.org/10.1038/292087a0
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DOI: https://doi.org/10.1038/292087a0
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