ArticleJournal of bacteriology1997
Leaderless polypeptides efficiently extracted from whole cells by osmotic shock.
Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 55 citations in OpenAlex.
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- Dropping Out and Other Fates of Transmembrane Segments Inserted by the SecA ATPase.Journal of molecular biology · 2019Article
- Improved in-cell structure determination of proteins at near-physiological concentration.Scientific reports · 2016Article
- Topology, dimerization, and stability of the single-span membrane protein CadC.Journal of molecular biology · 2014Article
- An approach to the production of soluble protein from a fungal gene encoding an aggregation-prone xylanase in Escherichia coli.PloS one · 2011Article
- NMR protein structure determination in living E. coli cells using nonlinear sampling.Nature protocols · 2010Article
- Effects of recombinant protein expression on green fluorescent protein diffusion in Escherichia coli.Biochemistry · 2009Article
- Article
- Structure of Bacillus subtilis superoxide dismutase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
- Translocation of alpha-synuclein expressed in Escherichia coli.Journal of bacteriology · 2007Article
- Functional similarities of a thermostable protein-disulfide oxidoreductase identified in the archaeon Pyrococcus horikoshii to bacterial DsbA enzymes.Extremophiles : life under extreme conditions · 2007Article
- Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Recognition of secretory proteins in Escherichia coli requires signals in addition to the signal sequence and slow folding.BMC microbiology · 2002Article
- Understanding the art of producing protein and nonprotein molecules in Escherichia coli.Molecular biotechnology · 2001Review
- Type II secretion by Aeromonas salmonicida: evidence for two periplasmic pools of proaerolysin.Journal of bacteriology · 2001Article
- Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins.Applied and environmental microbiology · 2001Article
- Secretion of recombinant proteins via the chaperone/usher pathway in Escherichia coli.Applied and environmental microbiology · 2001Article
- Molecular sieve mechanism of selective release of cytoplasmic proteins by osmotically shocked Escherichia coli.Journal of bacteriology · 2001Article
- Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin.Journal of bacteriology · 2000Article
- Membrane association of the Escherichia coli enterobactin synthase proteins EntB/G, EntE, and EntF.Journal of bacteriology · 2000Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three molecular foldases, DsbA, DsbC, and rotamase (ppiA), exhibited the unusual property of accumulating in an osmotically sensitive cellular compartment of Escherichia coli when their signal sequences were precisely removed by mutation. A mammalian protein, interleukin-1 (IL-1) receptor antagonist, behaved in a similar fashion in E. coli when its native signal sequence was deleted. These leaderless mutants (but not two control proteins overexpressed in the same system) were quantitatively extractable from whole cells by a variety of methods generally employed in the recovery of periplasmic proteins. A series of biochemical and genetic experiments showed that (i) leaderless DsbA (but not the wild type) was retained in a nonperiplasmic location; (ii) beta-galactosidase fusions to leaderless DsbA (but not to the wild type) exhibited efficient alpha complementation; (iii) none of the leaderless mutant proteins were substantially associated with cell membranes, even when they were overexpressed in cells; and (iv) leaderless DsbA was not transported to an osmotically sensitive compartment via a secA- or ftsZ-dependent mechanism. The observation that these proteins transit to some privileged cellular location by a previously undescribed mechanism(s)--absent their normal mode of (signal sequence-dependent) translocation--was unexpected. DsbA, rotamase, and IL-1, whose tertiary structures are known, appear to be structurally unrelated proteins. Despite a lack of obvious homologies, these proteins apparently have a common mechanism for intracellular localization. As this (putative) bacterial mechanism efficiently recognizes proteins of mammalian origin, it must be well conserved across evolutionary boundaries.
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