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 - PubMed (original) (raw)

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 et al. Proc Natl Acad Sci U S A. 1987 Dec.

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.

PubMed Disclaimer

References

1. Science. 1972 Nov 24;178(4063):871-2 -PubMed
1. J Biol Chem. 1987 Jul 5;262(19):9332-9 -PubMed
1. Methods Enzymol. 1975;42:504-11 -PubMed
1. J Virol. 1977 Mar;21(3):1128-39 -PubMed
1. J Biol Chem. 1977 May 25;252(10):3227-33 -PubMed

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 - PubMed (original) (raw)