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. 1987 Dec;84(23):8468–8472. doi: 10.1073/pnas.84.23.8468

Sec53, a protein required for an early step in secretory protein processing and transport in yeast, interacts with the cytoplasmic surface of the endoplasmic reticulum.

H Ruohola 1, S Ferro-Novick 1
PMCID: PMC299565  PMID: 3317409

Abstract

The sec53 mutant is a conditional lethal yeast secretory mutant. At 37 degrees C, precursors to exported proteins become firmly attached to the endoplasmic reticulum membrane and are not released into the lumen in a soluble form. The accumulated precursors are insoluble in the detergent Triton X-100; however, urea, a known protein denaturant, solubilizes them. Using antibody directed against the Sec53 protein, we found that a substantial portion of the Sec53 protein is associated with the cytoplasmic surface of the endoplasmic reticulum membrane. Membrane-bound Sec53 protein is largely insoluble in Triton X-100, but the protein is effectively released from the membrane by urea. We propose that the Sec53 protein may be a member of a complex of proteins required for an early step in protein processing and transport.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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