Abstract
Upon osmotic downshock, a few cytoplasmic proteins, including thioredoxin, elongation factor Tu (EF-Tu), and DnaK, are released from Tris-EDTA-treated Escherichia coli cells by an unknown mechanism. We have shown previously that deletion of mscL, the gene coding for the mechanosensitive channel of the plasma membrane with the highest conductance, prevents the release of thioredoxin. We confirm and extend the implication of MscL in this process by showing that the release of EF-Tu and DnaK is severely impaired in MscL-deficient strains. Release of these proteins is not observed in the absence of a Tris-EDTA treatment which disrupts the outer membrane, indicating that, in intact cells, they are transferred to the periplasm upon shock, presumably through the MscL channel.
MeSH Terms
Bacterial Proteins/metabolism
Biological Transport
Cytoplasm/metabolism
Escherichia coli/metabolism,physiology
Escherichia coli Proteins
HSP70 Heat-Shock Proteins/metabolism
Ion Channels/genetics,metabolism
Osmotic Pressure
Peptide Elongation Factor Tu/metabolism
Periplasm/metabolism
Chemicals
Bacterial Proteins
Escherichia coli Proteins
HSP70 Heat-Shock Proteins
Ion Channels
MscL protein, E coli
Peptide Elongation Factor Tu
dnaK protein, E coli
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Berrier C
Laboratoire des Biomembranes, UMR CNRS 8619, Université Paris-Sud, 91405 Orsay Cedex, France.
Garrigues A
Richarme G
Ghazi A
References (24)
24 references, click to expand
-
Abundance and membrane association of elongation factor Tu in E. coli.
Nature. 1976 May 6;261(5555):23-6
PMID: 775340
-
Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity.
EMBO J. 1999 Apr 1;18(7):1730-7
PMID: 10202137
-
Localization of thioredoxin from Escherichia coli in an osmotically sensitive compartment.
J Biol Chem. 1982 Oct 10;257(19):11424-30
PMID: 6811581
-
Association of thioredoxin with the inner membrane and adhesion sites in Escherichia coli.
J Bacteriol. 1987 Jun;169(6):2659-66
PMID: 3294802
-
A patch-clamp study of ion channels of inner and outer membranes and of contact zones of E. coli, fused into giant liposomes. Pressure-activated channels are localized in the inner membrane.
FEBS Lett. 1989 Dec 18;259(1):27-32
PMID: 2480919
-
Role of heat shock protein DnaK in osmotic adaptation of Escherichia coli.
J Bacteriol. 1991 Jul;173(14):4404-10
PMID: 2066337
-
Gadolinium ion inhibits loss of metabolites induced by osmotic shock and large stretch-activated channels in bacteria.
Eur J Biochem. 1992 Jun 1;206(2):559-65
PMID: 1350764
-
A large-conductance mechanosensitive channel in E. coli encoded by mscL alone.
Nature. 1994 Mar 17;368(6468):265-8
PMID: 7511799
-
Localization of DnaK (chaperone 70) from Escherichia coli in an osmotic-shock-sensitive compartment of the cytoplasm.
J Bacteriol. 1994 Nov;176(22):7074-8
PMID: 7961473
-
Multiple mechanosensitive ion channels from Escherichia coli, activated at different thresholds of applied pressure.
J Membr Biol. 1996 May;151(2):175-87
PMID: 8661505
-
Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli.
EMBO J. 1996 Sep 16;15(18):4798-805
PMID: 8890153
-
Mechanosensitive channels of Escherichia coli: the MscL gene, protein, and activities.
Annu Rev Physiol. 1997;59:633-57
PMID: 9074781
-
Cross-linking studies and membrane localization and assembly of radiolabelled large mechanosensitive ion channel (MscL) of Escherichia coli.
Biochem Biophys Res Commun. 1997 Mar 27;232(3):777-82
PMID: 9126353
-
Induction of heat shock proteins DnaK, GroEL, and GroES by salt stress in Lactococcus lactis.
Appl Environ Microbiol. 1997 May;63(5):1826-37
PMID: 9143115
-
Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli.
Biophys J. 1997 Oct;73(4):1925-31
PMID: 9336188
-
Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing.
J Biol Chem. 1997 Dec 19;272(51):32206-10
PMID: 9405422
-
Thioredoxin is an essential protein induced by multiple stresses in Bacillus subtilis.
J Bacteriol. 1998 Apr;180(7):1869-77
PMID: 9537387
-
Chaperone properties of bacterial elongation factor EF-Tu.
J Biol Chem. 1998 May 8;273(19):11478-82
PMID: 9565560
-
Mechanosensitive ion channels of the archaeon Haloferax volcanii.
J Biol Chem. 1998 May 15;273(20):12116-9
PMID: 9575156
-
Functional and structural conservation in the mechanosensitive channel MscL implicates elements crucial for mechanosensation.
Mol Microbiol. 1998 May;28(3):583-92
PMID: 9632260
-
Release of thioredoxin via the mechanosensitive channel MscL during osmotic downshock of Escherichia coli cells.
J Biol Chem. 1998 Oct 9;273(41):26670-4
PMID: 9756908
-
Protein-disulfide isomerase activity of elongation factor EF-Tu.
Biochem Biophys Res Commun. 1998 Nov 9;252(1):156-61
PMID: 9813162
-
Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel.
Science. 1998 Dec 18;282(5397):2220-6
PMID: 9856938
-
Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-TU, from Escherichia coli.
J Mol Biol. 1977 Dec 25;117(4):999-1012
PMID: 342708