Species-specificity of the BamA component of the bacterial outer membrane protein-assembly machinery.

Autor: Elena B Volokhina, Jan Grijpstra, Frank Beckers, Erika Lindh, Viviane Robert, Jan Tommassen, Martine P Bos

Publikováno v: PLoS ONE, Vol 8, Iss 12, p e85799 (2013)

The BamA protein is the key component of the Bam complex, the assembly machinery for outer membrane proteins (OMP) in gram-negative bacteria. We previously demonstrated that BamA recognizes its OMP substrates in a species-specific manner in vitro. In

Externí odkaz: https://doaj.org/article/66e90b2e9f89457ebf57f7921dca3f54

Lipidation of the autotransporter NalP of Neisseria meningitidis is required for its function in the release of cell-surface-exposed proteins

Autor: Peter van Ulsen, Jan Tommassen, Virginie Roussel-Jazédé, Vincent van Dam, Jan Grijpstra

Publikováno v: Roussel-Jazede, V, Grijpstra, J, van Dam, V, Tommassen, J & van Ulsen, P 2013, ' Lipidation of the autotransporter NalP of Neisseria meningitidis is required for its function in the release of cell-surface-exposed proteins ', Microbiology, vol. 159, pp. 286-95 . https://doi.org/10.1099/mic.0.063982-0
Microbiology, 159, 286-95. Microbiology Society

Autotransporters of Gram-negative bacteria consist of an N-terminal signal sequence, a C-terminal translocator domain and the secreted passenger domain in between. The autotransporter NalP of Neisseria meningitidis includes a protease domain that fac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c48eba9f3b866493096af69f1f27be10
https://doi.org/10.1099/mic.0.063982-0

Zinc Piracy as a Mechanism of Neisseria meningitidis for Evasion of Nutritional Immunity

Autor: Jan Poolman, Jan Grijpstra, Nathalie Devos, Jan Tommassen, Martine P. Bos, Michiel Stork, Carmen Mañas Torres, Walter J. Chazin

Publikováno v: PLoS Pathogens
PLoS Pathogens, Vol 9, Iss 10, p e1003733 (2013)

The outer membrane of Gram-negative bacteria functions as a permeability barrier that protects these bacteria against harmful compounds in the environment. Most nutrients pass the outer membrane by passive diffusion via pore-forming proteins known as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e53d65022a5e1daf184bffe2e01a8685
http://europepmc.org/articles/PMC3814407

Assembly of Bacterial Outer Membrane Proteins

Autor: Jan Grijpstra, Martine P. Bos, Jan Tommassen

Publikováno v: Methods in Molecular Biology ISBN: 9781627032445

Various methods that are routinely used to study the subcellular localization of membrane proteins in wild-type Gram-negative bacteria fall short in genetic studies addressing the biogenesis of outer membrane proteins (OMPs). Here, we describe three

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b29ac35b612d2f3fb65d0dd87b6c6de1
https://doi.org/10.1007/978-1-62703-245-2_14

Septal pore cap protein SPC18, isolated from the basidiomycetous fungus Rhizoctonia solani, also resides in pore plugs

Autor: Arie J. Verkleij, Arend F. van Peer, Wally H. Müller, Han A. B. Wösten, Kenneth G.A. van Driel, Teun Boekhout, Jan Grijpstra

Publikováno v: Eukaryotic Cell, 7(10), 1865-1873
Eukaryotic Cell 7 (2008) 10
Eukaryotic Cell, 7(10), 1865-1873. American Society for Microbiology

The hyphae of filamentous fungi are compartmentalized by septa that have a central pore. The fungal septa and septum-associated structures play an important role in maintaining cellular and intrahyphal homeostasis. The dolipore septa in the higher Ba

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86378cdcd48d184e5df61de4d3b15a0f
https://research.wur.nl/en/publications/septal-pore-cap-protein-spc18-isolated-from-the-basidiomycetous-f