Výsledky vyhledávání - "van der Does C"

DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island

Autor: Heilers, J.H., Reiners, J., Heller, E.M., Golzer, A., Smits, S.H.J., van der Does, C.

Publikováno v: 'Nucleic Acids Research ', vol: 47, pages: 8136-8153 (2019)

Relaxases of the MOBH family are often found on large plasmids, genetic islands and integrative conjugative elements. Many members of this family contain an N-terminal relaxase domain (TraI_2) followed by a disordered middle part and a C-terminal dom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=illesrfpubli::c88a88c88febe9c23b626f7a2b9a5344
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:53239

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The nucleotide-dependent interaction of FlaH and FlaI is essential for assembly and function of the archaellum motor

Autor: Chaudhury P, Neiner T, D'Imprima E, Banerjee A, Reindl S, Abhrajyoti Ghosh, As, Arvai, Dj, Mills, van der Does C, Ja, Tainer, Vonck J, Sv, Albers

Publikováno v: Molecular microbiology, vol 99, iss 4
Europe PubMed Central
Chaudhury, P; Neiner, T; D'Imprima, E; Banerjee, A; Reindl, S; Ghosh, A; et al.(2016). The nucleotide-dependent interaction of FlaH and FlaI is essential for assembly and function of the archaellum motor. Molecular Microbiology, 99(4), 674-685. doi: 10.1111/mmi.13260. Lawrence Berkeley National Laboratory: Lawrence Berkeley National Laboratory. Retrieved from: http://www.escholarship.org/uc/item/105165nf

© 2016 John Wiley & Sons Ltd. The motor of the membrane-anchored archaeal motility structure, the archaellum, contains FlaX, FlaI and FlaH. FlaX forms a 30nm ring structure that acts as a scaffold protein and was shown to interact with the bifunctio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::6c228321a1c7f5913e5d5327db000de1
https://escholarship.org/uc/item/105165nf

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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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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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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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