Functional characterization of the Escherichia coli K-12 yiaMNO transport protein genes

Autor: Plantinga, TH, van der Does, C, Badia, J, Aguilar, J, Konings, WN, Driessen, AJM, Plantinga, Titia H.

Publikováno v: Molecular Membrane Biology, 21(1), 51-57

The yiaMNO genes of Escherichia coli K-12 encode a binding protein-dependent secondary, or tri-partite ATP-independent periplasmic (TRAP), transporter. Since only a few members of this family have been functionally characterized to date, we aimed to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17a813912e407f42b6fdfdf58da49bcc
https://research.rug.nl/en/publications/494eede7-5611-4e75-8a07-9108772e19aa

The cell membrane and the struggle for life of lactic acid bacteria

Autor: Konings, WN

Publikováno v: Antonie Van Leeuwenhoek: International Journal of General and Molecular Microbiology, 82(1-4), 3-27. SPRINGER

The major life-threatening event for lactic acid bacteria (LAB) in their natural environment is the depletion of their energy sources and LAB can survive such conditions only for a short period of time. During periods of starvation LAB can exploit op

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::04e097f056bd4afae1e7d4169141a138
https://research.rug.nl/en/publications/e85ee03d-6f14-4d67-bf48-6ae22172cd42

How to distinguish between the vacuum cleaner and flippase mechanisms of the LmrA multi-drug transporter in Lactococcus lactis

Autor: Hofmeyr, JHS, Rohwer, JM, Snoep, JL, Westerhoff, HV, Konings, WN

Publikováno v: Molecular Biology Reports, 29(1-2), 107-112. SPRINGER

A numerical model of the LmrA multi-drug transport system of Lactococcus lactis is used to explore the possibility of distinguishing experimentally between two putative transport mechanisms, i.e., the vacuum-cleaner and the flippase mechanisms. This

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::51cf38dbd36c6782108b3876d9d2da09
https://research.rug.nl/en/publications/6e9c92c7-fa65-4b46-b9f4-ff9e158b95b3

Complementary metal ion specificity of the metal-citrate transporters CitM and CitH of Bacillus subtilis

Autor: Krom, BP, Warner, JB, Konings, WN, Lolkema, JS, Warner, Jessica B.

Publikováno v: Journal of Bacteriology, 182(22), 6374-81. American Society for Microbiology
Journal of Bacteriology, 182(22), 6374-6381. AMER SOC MICROBIOLOGY
Krom, B P, Warner, J B, Konings, W N & Lolkema, J S 2000, ' Complementary metal ion specificity of the metal-citrate transporters CitM and CitH of Bacillus subtilis ', Journal of Bacteriology, vol. 182, no. 22, pp. 6374-81 . https://doi.org/10.1128/JB.182.22.6374-6381.2000

Citrate uptake in Bacillus subtilis is stimulated by a wide range of divalent metal ions. The metal ions were separated into two groups based on the expression pattern of the uptake system. The two groups correlated with the metal ion specificity of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62800d3b9b95164cfaa0fcc76260d512
https://research.vu.nl/en/publications/63db4309-61db-4660-8b33-b00d282e7d1a

Catabolite repression and induction of the Mg2+-citrate transporter CitM of Bacillus subtilis

Autor: Warner, JB, Krom, BP, Magni, C, Konings, WN, Lolkema, JS, Warner, Jessica B.

Publikováno v: Journal of Bacteriology, 182(21), 6099-6105. AMER SOC MICROBIOLOGY

In Bacillus subtilis the citM gene encodes the Mg2+-citrate transporter. A target site for carbon catabolite repression (cre site) is located upstream of citM. Fusions of the citM promoter region, including the cre sequence, to the beta-galactosidase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::caefbbeb7e2a9e08f9230a36f736d44f
https://research.rug.nl/en/publications/40e88154-970d-40cb-9827-ff59527bcd58