Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli

Autor: E, Bouveret, R, Derouiche, A, Rigal, R, Lloubès, C, Lazdunski, H, Bénédetti

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1995, 270 (19), pp.11071-11077. ⟨10.1074/jbc.270.19.11071⟩
Journal of Biological Chemistry, 1995, 270 (19), pp.11071-11077. ⟨10.1074/jbc.270.19.11071⟩

International audience; TolA, -B, -Q, and -R proteins are involved in maintaining the cell envelope integrity of Escherichia coli; they have been parasitized by the group A colicins and the single strand DNA of some filamentous bacteriophages to perm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::bea1b5bb705799435c7284ed6a2ef802
https://hal.archives-ouvertes.fr/hal-02130195

Acidic interaction of the colicin A pore-forming domain with model membranes of Escherichia coli lipids results in a large perturbation of acyl chain order and stabilization of the bilayer

Autor: J. A. Killian, R. A. Demel, M. C. Koorengevel, Vincent Géli, C. Lazdunski

Publikováno v: Biochemistry. 31(45)

2H and 31P NMR techniques were used to study the effects on acyl chain order and lipid organization of the well-characterized pore-forming domain of colicin A (20-kDa thermolytic fragment of colicin A) upon insertion in model membrane systems derived

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c45e4a3fc019a42f81ddc1922e5b2dc0
https://pubmed.ncbi.nlm.nih.gov/1445847

The periseptal annulus in Escherichia coli

Autor: J. M. Pages, C. Lazdunski, Alain Bernadac, Jamila Anba

Publikováno v: Biology of the Cell. 50:273-277

Evidence is presented that two circumferential zones of cell envelope differentiation, the periseptal annuli, exist in E. coli as previously observed in S. typhimurium. The periseptal annulus is located at the division site of cells. A strain overpro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fae8ffb5d1d5c169e0bb28acd8efb4ba
https://doi.org/10.1111/j.1768-322x.1984.tb00274.x

Zn2+ and Co2+-Alkaline Phosphatases of E. coli. A Comparative Kinetic Study

Autor: C. Lazdunski, M. Lazdunski

Publikováno v: European Journal of Biochemistry. 7:294-300

1 For the Zn2+-phosphatase, the ratio k3/k2 (pH 8.4) of the dephosphorylation (k3) and phosphorylation (k2) rates is very similar, about 1.4–1.7, for substrates which are very different chemically such as p-nitrophenyl phosphate, β-glycerophosphat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b80b257a31d914f0c64f338753c5c189
https://doi.org/10.1111/j.1432-1033.1969.tb19606.x

Colicins are not transiently accumulated in the periplasmic space before release from colicinogenic cells

Autor: D. Cavard, Alain Bernadac, J. M. Pages, C. Lazdunski

Publikováno v: Biology of the cell. 51(1)

Colicins are released into the spent medium from colicinogenic cells. The pathway of release has been investigated in this study. The localization in producing cells of colicins A, E3 and of cloacin DF13 has been determined at various times after mit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05ceb1fe56d360a6147ec95c992d3bff
https://pubmed.ncbi.nlm.nih.gov/6237702