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Protein translocation pulls the plug

View Article: PubMed Central

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They find that a single SecY complex from Methanococcus jannaschii forms an hourglass-shaped pore with a basal plug that probably swings out of the way to let nascent protein chains pass... But more recent EM data are consistent with this supposed pore being only an indentation, and the new structure clearly suggests a path for nascent proteins through a single complex... Translocation begins, according to cross-linking data, when the signal sequence of the nascent protein inserts between transmembrane domains (TM) 2b and 7 of the main, channel-forming α-subunit... This probably has two effects... Further separation of the two halves should allow release of membrane-spanning domains of the nascent protein... The plug and pore ring are Rapoport's candidates for forming the tight seal that prevents passage of molecules other than the translocating protein... This sealing function had previously been ascribed to either the ribosome in the cytoplasm or (in eukaryotes) BiP in the lumen... Now, Rapoport needs to check that his presumed pore region is where the polypeptide really goes, and that the channel works in single copy and using the proposed plug movement... In the longer term he hopes to see the channel in action with a ribosome or even a translocating polypeptide; but for now, he says, seeing the current structure “has been a dream for me. ” ▪ Reference:

No MeSH data available.


A plug (green) stoppers the protein-conducting channel (seen from top).Rapoport/Macmillan
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uro1: A plug (green) stoppers the protein-conducting channel (seen from top).Rapoport/Macmillan


Protein translocation pulls the plug
A plug (green) stoppers the protein-conducting channel (seen from top).Rapoport/Macmillan
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2249868&req=5

uro1: A plug (green) stoppers the protein-conducting channel (seen from top).Rapoport/Macmillan

View Article: PubMed Central

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

They find that a single SecY complex from Methanococcus jannaschii forms an hourglass-shaped pore with a basal plug that probably swings out of the way to let nascent protein chains pass... But more recent EM data are consistent with this supposed pore being only an indentation, and the new structure clearly suggests a path for nascent proteins through a single complex... Translocation begins, according to cross-linking data, when the signal sequence of the nascent protein inserts between transmembrane domains (TM) 2b and 7 of the main, channel-forming α-subunit... This probably has two effects... Further separation of the two halves should allow release of membrane-spanning domains of the nascent protein... The plug and pore ring are Rapoport's candidates for forming the tight seal that prevents passage of molecules other than the translocating protein... This sealing function had previously been ascribed to either the ribosome in the cytoplasm or (in eukaryotes) BiP in the lumen... Now, Rapoport needs to check that his presumed pore region is where the polypeptide really goes, and that the channel works in single copy and using the proposed plug movement... In the longer term he hopes to see the channel in action with a ribosome or even a translocating polypeptide; but for now, he says, seeing the current structure “has been a dream for me. ” ▪ Reference:

No MeSH data available.