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Vol. 11, Issue 2, 765-772, February 2000
and
§
*Department of Cell Biology, Yale University School of Medicine,
New Haven, Connecticut 06520-8002; and Protein folding in the living cell begins cotranslationally. To
analyze how it is influenced by the ribosome and by the translocon complex during translocation into the endoplasmic reticulum, we expressed a mutant influenza hemagglutinin (a type I membrane glycoprotein) with a C-terminal extension. Analysis of the nascent chains by two-dimensional SDS-PAGE showed that ribosome attachment as
such had little effect on ectodomain folding or trimer assembly. However, as long as the chains were ribosome bound and
inside the translocon complex, formation of disulfides was partially suppressed, trimerization was inhibited, and the protein protected against aggregation.
Laboratory for
Biochemistry, Swiss Federal Institute of Technology, CH-8092 Zurich
Switzerland
Present address: Laboratory of Cell
Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10021.
§
Corresponding author. E-mail adddress:
ari.helenius{at}bc.biol.ethz.ch.
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