Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane

Kathrin Plath; Walter Mothes; Barrie M Wilkinson; Colin J Stirling; Tom A Rapoport

doi:10.1016/s0092-8674(00)81738-9

Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane

Kathrin Plath, Walter Mothes, Barrie M Wilkinson, Colin J Stirling, Tom A Rapoport

President and Vice-Chancellor

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Abstract

We have analyzed how the signal sequence of prepro-alpha-factor is recognized during the first step of posttranslational protein transport into the yeast endoplasmic reticulum. Cross-linking studies indicate that the signal sequence interacts in a Kar2p- and ATP-independent reaction with Sec61p, the multispanning membrane component of the protein-conducting channel, by intercalation into transmembrane domains 2 and 7. While bound to Sec61p, the signal sequence forms a helix that is contacted on one side by Sec62p and Sec71p. The binding site is located at the interface of the protein channel and the lipid bilayer. Signal sequence recognition in cotranslational translocation in mammals appears to occur similarly. These results suggest a general mechanism by which the signal sequence could open the channel for polypeptide transport.

Original language	English
Pages (from-to)	795-807
Number of pages	13
Journal	Cell
Volume	94
Issue number	6
DOIs	https://doi.org/10.1016/s0092-8674(00)81738-9
Publication status	Published - 1998

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title = "Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane",

abstract = "We have analyzed how the signal sequence of prepro-alpha-factor is recognized during the first step of posttranslational protein transport into the yeast endoplasmic reticulum. Cross-linking studies indicate that the signal sequence interacts in a Kar2p- and ATP-independent reaction with Sec61p, the multispanning membrane component of the protein-conducting channel, by intercalation into transmembrane domains 2 and 7. While bound to Sec61p, the signal sequence forms a helix that is contacted on one side by Sec62p and Sec71p. The binding site is located at the interface of the protein channel and the lipid bilayer. Signal sequence recognition in cotranslational translocation in mammals appears to occur similarly. These results suggest a general mechanism by which the signal sequence could open the channel for polypeptide transport.",

author = "Kathrin Plath and Walter Mothes and Wilkinson, {Barrie M} and Stirling, {Colin J} and Rapoport, {Tom A}",

year = "1998",

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T1 - Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane

AU - Plath, Kathrin

AU - Mothes, Walter

AU - Wilkinson, Barrie M

AU - Stirling, Colin J

AU - Rapoport, Tom A

PY - 1998

Y1 - 1998

N2 - We have analyzed how the signal sequence of prepro-alpha-factor is recognized during the first step of posttranslational protein transport into the yeast endoplasmic reticulum. Cross-linking studies indicate that the signal sequence interacts in a Kar2p- and ATP-independent reaction with Sec61p, the multispanning membrane component of the protein-conducting channel, by intercalation into transmembrane domains 2 and 7. While bound to Sec61p, the signal sequence forms a helix that is contacted on one side by Sec62p and Sec71p. The binding site is located at the interface of the protein channel and the lipid bilayer. Signal sequence recognition in cotranslational translocation in mammals appears to occur similarly. These results suggest a general mechanism by which the signal sequence could open the channel for polypeptide transport.

AB - We have analyzed how the signal sequence of prepro-alpha-factor is recognized during the first step of posttranslational protein transport into the yeast endoplasmic reticulum. Cross-linking studies indicate that the signal sequence interacts in a Kar2p- and ATP-independent reaction with Sec61p, the multispanning membrane component of the protein-conducting channel, by intercalation into transmembrane domains 2 and 7. While bound to Sec61p, the signal sequence forms a helix that is contacted on one side by Sec62p and Sec71p. The binding site is located at the interface of the protein channel and the lipid bilayer. Signal sequence recognition in cotranslational translocation in mammals appears to occur similarly. These results suggest a general mechanism by which the signal sequence could open the channel for polypeptide transport.

U2 - 10.1016/s0092-8674(00)81738-9

DO - 10.1016/s0092-8674(00)81738-9

M3 - Article

SN - 0092-8674

VL - 94

SP - 795

EP - 807

JO - Cell

JF - Cell

IS - 6

ER -

Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane

Abstract

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