Genetics and biochemistry of the assembly of proteins into the outer membrane of E. coli.
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- Type
- review
- Published
- 1987-01-01
- Cited by
- 28
- References
- 135
- Access
- Open access
- OpenAlex
- https://openalex.org/W1979616768
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:8916785
Keywords
Bacterial outer membrane, Membrane protein, Biochemistry, Biology, Chemistry
References
- Intragenic regions required for LamB export.
- Evidence for posttranslational translocation of beta-lactamase across the bacterial inner membrane.
- Precursor forms of penicillin-binding proteins 5 and 6 of E. coli cytoplasmic membrane
- An inner membrane protein N‐terminal signal sequence is able to promote efficient localisation of an outer membrane protein in Escherichia coli.
- The C terminus of penicillin‐binding protein 5 is essential for localisation to the E. coli inner membrane.
- Translocation of nascent secretory proteins across membranes can occur late in translation.
- In vitro translocation of protein across Escherichia coli membrane vesicles requires both the proton motive force and ATP.
- Recombinant forms of M13 procoat with an OmpA leader sequence or a large carboxy‐terminal extension retain their independence of secY function.
- Absence of ferric enterobactin receptor modification activity in mutants of Escherichia coli K-12 lacking protein a.
- The secY protein can act post-translationally to promote bacterial protein export.
- The requirement for energy during export of beta‐lactamase in Escherichia coli is fulfilled by the total protonmotive force.
- Signal recognition particle (SRP) does not mediate a translational arrest of nascent secretory proteins in mammalian cell‐free systems.
- Both hydrophobic domains of M13 procoat are required to initiate membrane insertion.
- Transport of vitamin B12 in Escherichia coli: common receptor system for vitamin B12 and bacteriophage BF23 on the outer membrane of the cell envelope
- Mechanism of signal peptide cleavage in the biosynthesis of the major lipoprotein of the Escherichia coli outer membrane.
- Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli.
- ompT: Escherichia coli K-12 Structural Gene for Protein a (3b)
- Genetic Analysis of Components Involved in Vitamin B12 Uptake in Escherichia coli
- Both linked and unlinked mutations can alter the intracellular site of synthesis of exported proteins of Escherichia coli
- Intermediate location in the assembly of the matrix protein or porin into the outer membrane of Escherichia coli
Cited by
- Expert system for predicting protein localization sites in gram‐negative bacteria
- Specific regions of Escherichia coli OmpF protein involved in antigenic and colicin receptor sites and in stable trimerization
- OmpF assembly mutants of Escherichia coli K-12: isolation, characterization, and suppressor analysis
- Assembly of LamB and OmpF in deep rough lipopolysaccharide mutants of Escherichia coli K-12
- Interactions between folding factors and bacterial outer membrane proteins
- Probing FhuA‘-’PhoA fusion proteins for the study of FhuA export into the cell envelope of Escherichia coli K12
- Protein translocation in Escherichia coli.
- Secretion of active β-lactamase to the medium mediated by the Escherichia coli haemolysin transport pathway
- Secretion of Ricinus communis glyceraldehyde‐3‐phosphate dehydrogenase by Escherichia coli
- Dynamics of the exposure of epitopes on OmpF, an outer membrane protein of Escherichia coli.
- Involvement of exposed polypeptide loops in trimeric stability and membrane insertion of Escherichia coli OmpF porin.
- Immunological approach of assembly and topology of OmpF, an outer membrane protein of Escherichia coli.
- A genetic engineering approach to study the mode of assembly of the OmpF porin in the envelope of E coli.
- asmB, a suppressor locus for assembly-defective OmpF mutants of Escherichia coli, is allelic to envA (lpxC)
- Intragenic Suppressors of an OmpF Assembly Mutant and Assessment of the Roles of Various OmpF Residues in Assembly through Informational Suppressors
- Streptokinase mutations relieving Escherichia coli K-12 (prlA4) of detriments caused by the wild-type skc gene
- Using codon usage to predict genes origin: is the Escherichia coli outer membrane a patchwork of products from different genomes?
- Inhibition of PhoE translocation across Escherichia coli inner-membrane vesicles by synthetic signal peptides suggests an important role of acidic phospholipids in protein translocation.
- Prevalence of outer membrane porin alteration in beta-lactam-antibiotic-resistant Enterobacter aerogenes
- Overexpression of Protease-Deficient DegPS210ARescues the Lethal Phenotype of Escherichia coli OmpF Assembly Mutants in a degP Background
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