Zobrazeno 1 - 10 of 307 pro vyhledávání: '"DRIESSEN, AJM"'
1
The oligomeric distribution of SecYEG is altered by SecA and translocation ligands
Autor: Scheuring, J, Braun, N, Nothdurft, L, Stumpf, M, Veenendaal, AKJ, Kol, S, van der Does, C, Driessen, AJM, Weinkauf, S, Veenendaal, Andreas K.J.
Publikováno v: Journal of Molecular Biology, 354(2), 258-271. Academic Press
The multimeric membrane protein complex translocase mediates the transport of preproteins across and integration of membrane proteins into the inner membrane of Escherichia coli. The translocase consists of the peripheral membrane-associated ATPase S
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::858c07edae56ad1f35fdfe00e463a071
https://hdl.handle.net/11370/10e3562f-2ab2-4ef0-911b-9acc3a40a54e
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2
Functional and structural characterization of the minimal Sec translocase of the hyperthermophile Thermotoga maritima
Autor: Pretz, MG, Remigy, H, Swaving, J, Albers, SV, Garrido, VG, Chami, M, Engel, A, Driessen, AJM, Pretz, Monika G., Garrido, Victoria G.
Publikováno v: Extremophiles, 9(4), 307-316
The genome of the hyperthermophilic bacterium Thermotoga maritima contains the genes that encode core subunits of the protein translocase, a complex consisting of the molecular motor SecA and the protein conducting pore SecYE. In addition, we identif
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15b698c90d7f3f1997a4cadfc96a8432
https://doi.org/10.1007/s00792-005-0446-3
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3
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
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4
Formation of the Productive ATP-Mg 2+ -bound Dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus
Autor: Verdon, G, Albers, SV, van Oosterwijk, N, Dijkstra, BW, Driessen, AJM, Thunnissen, AMWH, Dijkstra, Bauke W.
Publikováno v: Journal of Molecular Biology, 334(2), 255-267. Academic Press
The ABC-ATPase GlcV from Sulfolobus solfataricus energizes an ABC transporter mediating glucose uptake. In ABC transporters, two ABC-ATPases are believed to form a head-to-tail dimer, with both monomers contributing conserved residues to each of the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8340a720a8b526bd69c1fb1d8a78c357
https://doi.org/10.1016/j.jmb.2003.08.065
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5
Proton motive force-dependent Hoechst 33342 transport by the ABC transporter LmrA of Lactococcus lactis
Autor: van Saparoea, HBV, Lubelski, J, van Merkerk, R, Mazurkiewicz, PS, Driessen, AJM, Mazurkiewicz, Piotr S.
Publikováno v: Biochemistry, 44(51), 16931-16938. AMER CHEMICAL SOC
The fluorescent compound Hoechst 33342 is a substrate for many multidrug resistance (MDR) transporters and is widely used to characterize their transport activity. We have constructed mutants of the adenosine triphosphate (ATP) binding cassette (ABC)
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::930dea6d836121412876c518dd1ebd1f
https://pubmed.ncbi.nlm.nih.gov/16363806
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7
Covalently dimerized SecA is functional in protein translocation
Autor: de Keyzer, J, van der Sluis, EO, Spelbrink, REJ, Nijstad, N, de Kruijff, B, Nouwen, N, van der Does, C, Driessen, AJM, Sluis, Eli O. van der, Spelbrink, Robin E.J.
Publikováno v: The Journal of Biological Chemistry, 280(42), 35255-35260. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
The ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli. SecA exists as a dimer in solution, but the exact oligomeric state of SecA during membrane binding and preprotein
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6e0aeaceb72a38eb69d3a540190fc6e
https://research.rug.nl/en/publications/dd386df2-6c5c-4360-9266-b9275b896854
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9
Conditional lethal mutations separate the M13 procoat and Pf3 coat functions of YidC - Different YidC structural requirements for membrane protein insertion
Autor: Chen, MY, Xie, K, Nouwen, N, Driessen, AJM, Dalbey, RE, Dalbey, Ross E.
Publikováno v: The Journal of Biological Chemistry, 278(26), 23295-23300. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Conditional lethal YidC mutants have been isolated to decipher the role of YidC in the assembly of Sec-dependent and Sec-independent membrane proteins. We now show that the membrane insertion of the Sec-independent M13 procoat-lep protein is inhibite
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::89793118ced1e306d562fe24b2052987
https://research.rug.nl/en/publications/3bb188ab-295d-413f-8a02-8d0d80192299
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10
LYSINE-106 OF THE PUTATIVE CATALYTIC ATP-BINDING SITE OF THE BACILLUS-SUBTILIS SECA PROTEIN IS REQUIRED FOR FUNCTIONAL COMPLEMENTATION OF ESCHERICHIA-COLI SECA MUTANTS INVIVO
Autor: Klose, M., Schimz, Kl, Vanderwolk, J., Driessen, Ajm, Roland Freudl
Publikováno v: The Journal of Biological Chemistry, 268(6), 4504-4510. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
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The SecA protein is a major component of the cellular machinery that mediates the translocation of proteins across the Escherichia coli plasma membrane. The secA gene from Bacillus subtilis was cloned and expressed in E. coli under the control of the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::a5c1f18e932346ac562f467c40637501
https://research.rug.nl/en/publications/6a684275-7f8b-40a4-b097-9fd0d53e1112
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