ArticleJournal of bacteriology1999
Mapping an interface of SecY (PrlA) and SecE (PrlG) by using synthetic phenotypes and in vivo cross-linking.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
40 citing papers in PubMed, 105 citations in OpenAlex.
- Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023Review
- Stepwise gating of the Sec61 protein-conducting channel by Sec63 and Sec62.Nature structural & molecular biology · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Genetic Analysis of Protein Translocation.The protein journal · 2019Review
- Crosslinking and Reconstitution Approaches to Study Protein Transport.The protein journal · 2019Review
- Dynamic action of the Sec machinery during initiation, protein translocation and termination.eLife · 2018Article
- Article
- Channel crossing: how are proteins shipped across the bacterial plasma membrane?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Emerging themes in SecA2-mediated protein export.Nature reviews. Microbiology · 2012Review
- The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Position-dependent effects of polylysine on Sec protein transport.The Journal of biological chemistry · 2012Article
- Structure of the SecY complex unlocked by a preprotein mimic.Cell reports · 2012Article
- Conformational dynamics of the plug domain of the SecYEG protein-conducting channel.The Journal of biological chemistry · 2011Article
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
- Preserving the membrane barrier for small molecules during bacterial protein translocation.Nature · 2011Article
- Immobilization of the plug domain inside the SecY channel allows unrestricted protein translocation.The Journal of biological chemistry · 2010Article
- The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration.Molecular biology of the cell · 2010Article
- Mapping polypeptide interactions of the SecA ATPase during translocation.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- The SecY complex forms a channel capable of ionic discrimination.EMBO reports · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
SecY and SecE are integral cytoplasmic membrane proteins that form an essential part of the protein translocation machinery in Escherichia coli. Sites of direct contact between these two proteins have been suggested by the allele-specific synthetic phenotypes exhibited by pairwise combinations of prlA and prlG signal sequence suppressor mutations in these genes. We have introduced cysteine residues within the first periplasmic loop of SecY and the second periplasmic loop of SecE, at a specific pair of positions identified by this genetic interaction. The expression of the cysteine mutant pair results in a dominant lethal phenotype that requires the presence of DsbA, which catalyzes the formation of disulfide bonds. A reducible SecY-SecE complex is also observed, demonstrating that these amino acids must be sufficiently proximal to form a disulfide bond. The use of cysteine-scanning mutagenesis enabled a second contact site to be discovered. Together, these two points of contact allow the modeling of a limited region of quaternary structure, establishing the first characterized site of interaction between these two proteins. This study proves that actual points of protein-protein contact can be identified by using synthetic phenotypes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.