Genomics

Dataset Information

39

The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins


ABSTRACT: The endoplasmic reticulum (ER) supports biosynthesis of proteins with diverse transmembrane domain (TMD) lengths and hydrophobicity. Features in transmembrane domains such as charged residues in ion channels are often functionally important, but could pose a challenge during cotranslational membrane insertion and folding. Our systematic proteomic approaches in both yeast and human cells revealed that the ER membrane protein complex (EMC) binds to and promotes the biogenesis of a range of multipass transmembrane proteins, with a particular enrichment for transporters. Proximity-specific ribosome profiling demonstrates that the EMC engages clients cotranslationally and immediately following clusters of TMDs enriched for charged residues. The EMC can remain associated after completion of translation, which both protects clients from premature proteasomal degradation and allows recruitment of substrate-specific and general chaperones. Thus, the EMC broadly enables the biogenesis of multipass transmembrane proteins containing destabilizing features, thereby mitigating the trade-off between function and stability. Overall design: Ribosome profiling of whole cell or streptavidin-purified ribosomes biotinylated by ER-localized biotin ligase in yeast This series includes re-analyzed samples from GSE61012 and GSE85686.

INSTRUMENT(S): Illumina HiSeq 2000 (Saccharomyces cerevisiae)

SUBMITTER: Jonathan S Weissman 

PROVIDER: GSE112891 | GEO | 2018-05-29

REPOSITORIES: GEO

Dataset's files

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Action DRS
GSE112891_HeLa_RPKMs.txt.gz Txt
GSE112891_yeast_codon_counts.txt.gz Txt
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The endoplasmic reticulum (ER) supports biosynthesis of proteins with diverse transmembrane domain (TMD) lengths and hydrophobicity. Features in transmembrane domains such as charged residues in ion channels are often functionally important, but could pose a challenge during cotranslational membrane insertion and folding. Our systematic proteomic approaches in both yeast and human cells revealed that the ER membrane protein complex (EMC) binds to and promotes the biogenesis of a range of multipa  ...[more]

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