Elongation Factor Tu and DnaK Are Transferred from the Cytoplasm to the Periplasm of Escherichia coli during Osmotic Downshock Presumably via the Mechanosensitive Channel MscL
- 1 January 2000
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 182 (1), 248-251
- https://doi.org/10.1128/jb.182.1.248-251.2000
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.Keywords
This publication has 22 references indexed in Scilit:
- Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activityThe EMBO Journal, 1999
- Protein–Disulfide Isomerase Activity of Elongation Factor EF-TuBiochemical and Biophysical Research Communications, 1998
- Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coliBiophysical Journal, 1997
- MECHANOSENSITIVE CHANNELS OFESCHERICHIA COLI:The MscL Gene, Protein, and ActivitiesAnnual Review of Physiology, 1997
- Multiple Mechanosensitive Ion Channels from Escherichia coli, Activated at Different Thresholds of Applied PressureThe Journal of Membrane Biology, 1996
- A large-conductance mechanosensitive channel in E. coli encoded by mscL aloneNature, 1994
- Gadolinium ion inhibits loss of metabolites induced by osmotic shock and large stretch‐activated channels in bacteriaEuropean Journal of Biochemistry, 1992
- A patch‐clamp study of ion channels of inner and outer membranes and of contact zones of E. coli, fused into giant liposomesFEBS Letters, 1989
- Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-Tu, from Escherichia coliJournal of Molecular Biology, 1977
- Abundance and membrane association of elongation factor Tu in E. coliNature, 1976