ArticleProceedings of the National Academy of Sciences of the United States of America2003
SecA-dependent quality control of intracellular protein localization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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.
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Who cites it
14 citing papers in PubMed.
- Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity.Scientific reports · 2022Article
- Coexpressing the Signal Peptide of Vip3A and the Trigger Factor ofFrontiers in microbiology · 2022Article
- Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.EMBO reports · 2020Article
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
- The Tat Substrate CueO Is Transported in an Incomplete Folding State.The Journal of biological chemistry · 2016Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- SecA is required for membrane targeting of the cell division protein DivIVA in vivo.Frontiers in microbiology · 2014Article
- Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Journal of bacteriology · 2013Article
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
- Interactions that drive Sec-dependent bacterial protein transport.Biochemistry · 2007Review
- Oligomeric states of the SecA and SecYEG core components of the bacterial Sec translocon.Biochimica et biophysica acta · 2007Review
- Target-directed proteolysis at the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- A little help from my friends: quality control of presecretory proteins in bacteria.Journal of bacteriology · 2004Review
- SecB is a bona fide generalized chaperone in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complex secretion machineries mediate protein translocation across cellular membranes. These machines typically recognize their substrates via signal sequences, which are required for proper targeting to the translocon. We report that during posttranslational secretion the widely conserved targeting factor SecA performs a quality-control function that is based on a general chaperone activity. This quality-control mechanism involves assisted folding of signal sequenceless proteins, thereby excluding them from the secretion process. These results suggest that SecA channels proteins into one of two key pathways, posttranslational secretion or folding in the cytoplasm. Implications of this finding for intracellular protein localization are discussed.
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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.