Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Robert J. Brooker"'
Publikováno v:
Journal of Membrane Biology. 211:101-113
Four amino acids critical for lactose permease function were altered using site-directed mutagenesis. The resulting Quad mutant (E269Q/R302L/H322Q/E325Q) was expressed at 60% of wild-type levels but found to have negligible transport activity. The Qu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ac2db77b68656e1c4ca8b41df6c0089
https://doi.org/10.1007/s00232-005-7020-x
https://doi.org/10.1007/s00232-005-7020-x
Publikováno v:
Journal of Membrane Biology. 201:97-107
A bioinformatic approach was used for the identification of residues that are conserved within the Nramp family of metal transporters. Site-directed mutagenesis was then carried out to change six conserved acidic residues (i.e., Asp-34, Glu-102, Asp-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df2e0d1184408d8719a594ac0eaffdc5
https://doi.org/10.1007/s00232-004-0711-x
https://doi.org/10.1007/s00232-004-0711-x
Autor:
Jerry L. Johnson, Robert J. Brooker
Publikováno v:
Journal of Membrane Biology. 198:135-146
A combinatorial approach was used to study putative interactions among six ionizable residues (Asp-240, Glu-269, Arg-302, Lys-319, His-322, and Glu-325) in the lactose permease. Neutral mutations were made involving five ion pairs that had not been p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7def549969bc992deb41e73bd3aafcdb
https://doi.org/10.1007/s00232-004-0667-x
https://doi.org/10.1007/s00232-004-0667-x
Publikováno v:
Biochemistry. 42:11226-11233
Previous work on the lactose permease of Escherichia coli has shown that mutations along a face of predicted transmembrane segment 8 (TMS-8) play a critical role in conformational changes associated with lactose transport (Green, A. L., and Brooker,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::46e00273f306081b8dcee5b751c2dcd5
https://doi.org/10.1021/bi034810+
https://doi.org/10.1021/bi034810+
Publikováno v:
Anal. Methods. 4:44-46
A facile activity assay for an H+-coupled transporter using florescent probes was developed with an H+-coupled manganese transporter (MntH) as a model. Making use of coupled-proton transport, the transport activity (H+/Mn2+ cotransport) can be direct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2b367fc8b4647a45d5c44c8003fdb96d
https://doi.org/10.1039/c1ay05549f
https://doi.org/10.1039/c1ay05549f
Autor:
Robert J. Brooker, Aileen L. Green
Publikováno v:
Biochemistry. 40:12220-12229
Previous work on the lactose permease of Escherichia coli has shown that mutations along a face of predicted transmembrane segment 2 (TMS-2) play a critical role in conformational changes associated with lactose transport [Green, A. L., Anderson, E.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f4c5aef7c12817a0c761425f462a912
https://doi.org/10.1021/bi0109055
https://doi.org/10.1021/bi0109055
Publikováno v:
The Journal of Membrane Biology. 181:215-224
In a previous study, we characterized a lactose permease mutant (K319N/E325Q) that can transport H+ ions with sugar. This result was surprising because other studies had suggested that Glu-325 plays an essential role in H+ binding. To determine if th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d21a8f8e81b7b37eb54b1bd564734c2
https://doi.org/10.1007/s00232-001-0024-2
https://doi.org/10.1007/s00232-001-0024-2
Publikováno v:
Journal of Biological Chemistry. 275:28695-28700
In chemiosmotic coupling, a transmembrane ion gradient is used as the source of energy to drive reactions. This process occurs in all cells, but the microscopic mechanism is not understood. Here, Escherichia coli lactose permease was used in a novel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3f3e6a5ac23bccc037da54cdae639946
https://doi.org/10.1074/jbc.m005129200
https://doi.org/10.1074/jbc.m005129200
Publikováno v:
The Journal of Membrane Biology. 176:159-168
The major facilitator superfamily (MFS) of transport proteins, which includes the lactose permease of Escherichia coli, contains a conserved motif G-X-X-X-D/E-R/K-X-G-R/K-R/K in the loops that connect transmembrane segments 2 and 3, and transmembrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aa42c0482f97a4fe1ae1568c7d0b1a1
https://doi.org/10.1007/s00232001085
https://doi.org/10.1007/s00232001085
Publikováno v:
Biochemistry. 37:15363-15375
The lactose permease, encoded by the lacY gene of Escherichia coli, is an integral membrane protein that functions as a proton and lactose symporter. In this study, we have characterized a novel monodisperse, purified preparation of lactose permease,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d5a54e560540d47cbe0e8762e1c22b7
https://doi.org/10.1021/bi981142x
https://doi.org/10.1021/bi981142x