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Vol. 9, Issue 12, 3455-3473, December 1998
*Howard Hughes Medical Institute and Department of Molecular Cell
Biology, University of California at Berkeley, Berkeley California
94720; and
The evolutionarily conserved Sec61 protein complex mediates the
translocation of secretory proteins into the endoplasmic reticulum. To
investigate the role of Sec61p, which is the main subunit of this
complex, we generated recessive, cold-sensitive alleles of sec61 that encode stably expressed proteins with strong
defects in translocation. The stage at which posttranslational
translocation was blocked was probed by chemical crosslinking of
radiolabeled secretory precursors added to membranes isolated from
wild-type and mutant strains. Two classes of sec61
mutants were distinguished. The first class of mutants was defective in
preprotein docking onto a receptor site of the translocon that included
Sec61p itself. The second class of mutants allowed docking of
precursors onto the translocon but was defective in the ATP-dependent
release of precursors from this site that in wild-type membranes leads to pore insertion and full translocation. Only mutants of the second
class were partially suppressed by overexpression of
SEC63, which encodes a subunit of the Sec61 holoenzyme
complex responsible for positioning Kar2p (yeast BiP) at the
translocation channel. These mutants thus define two early stages of
translocation that require SEC61 function before
precursor protein transfer across the endoplasmic reticulum membrane.
Medical Research Council Laboratory for
Molecular Cell Biology and Department of Biochemistry, University
College London, London WC1E 6BT, United Kingdom
Present address: Department of Biology,
Colorado State University, Anatomy/Zoology Building, Fort Collins, CO 80523.
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