ArticleEMBO reports2009
The SecY complex forms a channel capable of ionic discrimination.
Article in EMBO reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Adaptive Evolution ofMicroorganisms · 2025Article
- Article
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023Review
- Article
- A unified evolutionary origin for the ubiquitous protein transporters SecY and YidC.BMC biology · 2021Article
- Profiling theeLife · 2019Article
- Investigating the stability of the SecA-SecYEG complex during protein translocation across the bacterial membrane.The Journal of biological chemistry · 2019Article
- Driving Forces of Translocation Through Bacterial Translocon SecYEG.The Journal of membrane biology · 2018Article
- A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Article
- Ion conductivity of the bacterial translocation channel SecYEG engaged in translocation.The Journal of biological chemistry · 2014Article
- Escherichia coli membranes depleted of SecYEG elicit SecA-dependent ion-channel activity but lose signal peptide specificity.The Journal of membrane biology · 2012Article
- Structure-activity analysis of niclosamide reveals potential role for cytoplasmic pH in control of mammalian target of rapamycin complex 1 (mTORC1) signaling.The Journal of biological chemistry · 2012Article
- Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Preserving the membrane barrier for small molecules during bacterial protein translocation.Nature · 2011Article
- The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration.Molecular biology of the cell · 2010Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein translocation across the bacterial membrane occurs at the SecY complex or channel. The resting SecY channel is impermeable to small molecules owing to a plug domain that creates a seal. Here, we report that a channel loosely sealed, or with a plug locked open, does not, however, lead to general membrane permeability. Instead, strong selectivity towards small monovalent anions, especially chloride, is observed. Mutations in the pore ring-structure increase both the translocation activity of the channel and its ionic conductance, however the selectivity is maintained. The same ionic specificity also occurs at the onset of protein translocation and across the archaeal SecY complex. Thus, the ion-conducting characteristic of the channel seems to be conserved as a normal consequence of protein translocation. We propose that the pore ring-structure forms a selectivity filter, allowing cells to tolerate channels with imperfect plugs.
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