ArticleThe EMBO journal1996
Targeting of signal sequenceless proteins for export in Escherichia coli with altered protein translocase.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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Who cites it
26 citing papers in PubMed, 64 citations in OpenAlex.
- Functional mapping and engineering of the Sec translocon unlocked by a cell-free system.Science advances · 2026Article
- A small molecule allosterically activates SecA dependent secretion.Communications biology · 2026Article
- Roles of Mature Domain Targeting Signals (MTSs) for Protein Translocation and Secretion inInternational journal of molecular sciences · 2024Article
- Evolutionary adaptation of the protein folding pathway for secretability.The EMBO journal · 2022Article
- SecY-mediated quality control prevents the translocation of non-gated porins.Scientific reports · 2020Article
- Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.EMBO reports · 2020Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
- SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo.Journal of bacteriology · 2017Article
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- Heat shock transcription factor σ32 co-opts the signal recognition particle to regulate protein homeostasis in E. coli.PLoS biology · 2013Article
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- Interactions that drive Sec-dependent bacterial protein transport.Biochemistry · 2007Review
- Investigating the SecY plug movement at the SecYEG translocation channel.The EMBO journal · 2005Article
- Modeling the effects of prl mutations on the Escherichia coli SecY complex.Journal of bacteriology · 2005Article
- A little help from my friends: quality control of presecretory proteins in bacteria.Journal of bacteriology · 2004Review
- Protein quality control in the bacterial periplasm.Microbial cell factories · 2004Article
- SecA-dependent quality control of intracellular protein localization.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Recognition of secretory proteins in Escherichia coli requires signals in addition to the signal sequence and slow folding.BMC microbiology · 2002Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most extracytoplasmic proteins are synthesized with an N-terminal signal sequence that targets them to the export apparatus. Escherichia coli prlA mutants (altered in the secY gene) are able to export cell envelope proteins lacking any signal sequence. In order to understand how such proteins are targeted for export, we isolated mutations in a signal sequenceless version of alkaline phosphatase that block its export in a prlA mutant. The mutations introduce basic amino acyl residues near the N-terminus of alkaline phosphatase. These changes do not disrupt an N-terminal export signal in this protein since the first 25 amino acids can be removed without affecting its export competence. These findings suggest that signal sequenceless alkaline phosphatase does not contain a discrete domain that targets it for export and may be targeted simply because it remains unfolded in the cytoplasm. We propose that basic amino acids near the N-terminus of a signal sequenceless protein affect its insertion into the translocation apparatus after it has been targeted for export. These findings allow the formulation of a model for the entry of proteins into the membrane-embedded export machinery.
Indexed as
Identifiers
8895566PMC452265W1276010910What OpenQuestion holds
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.