ArticleJournal of bacteriology2000
The net charge of the first 18 residues of the mature sequence affects protein translocation across the cytoplasmic membrane of gram-negative bacteria.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Who cites it
22 citing papers in PubMed.
- Signal Peptides: From Molecular Mechanisms to Applications in Protein and Vaccine Engineering.Biomolecules · 2025Review
- New Perspectives on Escherichia coli Signal Peptidase I Substrate Specificity: Investigating Why the TasA Cleavage Site Is Incompatible with LepB Cleavage.Microbiology spectrum · 2023Article
- Effect of Secretion Efficiency of Mutant KRAS Neoantigen byInternational journal of molecular sciences · 2023Article
- Optimization of Signal Peptide via Site-Directed Mutagenesis for Enhanced Secretion of Heterologous Proteins inInternational journal of molecular sciences · 2022Article
- Synthetic pro-peptide design to enhance the secretion of heterologous proteins by Saccharomyces cerevisiae.MicrobiologyOpen · 2022Article
- Understanding the mammalian TRAP complex function(s).Open biology · 2020Review
- SecA mediates cotranslational targeting and translocation of an inner membrane protein.The Journal of cell biology · 2017Article
- MatureP: prediction of secreted proteins with exclusive information from their mature regions.Scientific reports · 2017Article
- The code for directing proteins for translocation across ER membrane: SRP cotranslationally recognizes specific features of a signal sequence.Journal of molecular biology · 2015Article
- Expression and efficient secretion of a functional chitinase from Chromobacterium violaceum in Escherichia coli.BMC biotechnology · 2013Article
- Signal peptidase I: cleaving the way to mature proteins.Protein science : a publication of the Protein Society · 2012Review
- The extended signal peptide of the trimeric autotransporter EmaA of Aggregatibacter actinomycetemcomitans modulates secretion.Journal of bacteriology · 2011Article
- Dissection of an old protein reveals a novel application: domain D of Staphylococcus aureus Protein A (sSpAD) as a secretion--tag.Microbial cell factories · 2010Article
- Export of a hyperexpressed mammalian globular cytochrome b5 precursor in Escherichia coli is dramatically affected by the nature of the amino acid flanking the secretory signal sequence cleavage bond.Protein science : a publication of the Protein Society · 2010Article
- Rational design of a fusion partner for membrane protein expression in E. coli.Protein science : a publication of the Protein Society · 2009Article
- Identification of a post-targeting step required for efficient cotranslational translocation of proteins across the Escherichia coli inner membrane.The Journal of biological chemistry · 2009Article
- A novel Ecotin-Ubiquitin-Tag (ECUT) for efficient, soluble peptide production in the periplasm of Escherichia coli.Microbial cell factories · 2009Article
- Flanking signal and mature peptide residues influence signal peptide cleavage.BMC bioinformatics · 2008Article
- Review
- Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides.The Journal of biological chemistry · 2007Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
This statistical study shows that in proteins of gram-negative bacteria exported by the Sec-dependent pathway, the first 14 to 18 residues of the mature sequences have the highest deviation between the observed and expected net charge distributions. Moreover, almost all sequences have either neutral or negative net charge in this region. This rule is restricted to gram-negative bacteria, since neither eukaryotic nor gram-positive bacterial exported proteins have this charge bias. Subsequent experiments performed with a series of Escherichia coli alkaline phosphatase mutants confirmed that this charge bias is associated with protein translocation across the cytoplasmic membrane. Two consecutive basic residues inhibit translocation effectively when placed within the first 14 residues of the mature protein but not when placed in positions 19 and 20. The sensitivity to arginine partially reappeared again 30 residues away from the signal sequence. These data provide new insight into the mechanism of protein export in gram-negative bacteria and lead to practical recommendations for successful secretion of hybrid proteins.
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