Výsledky vyhledávání - "Robert M. Macnab"

Akademický článek

Obituary Robert M. Macnab.

Autor: Grindley, Nigel D. F.

Publikováno v: Molecular Microbiology; Jan2004, Vol. 51 Issue 1, p1-2, 2p, 1 Black and White Photograph

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The Type III Flagellar Export Specificity Switch is Dependent on FliK Ruler and a Molecular Clock

Autor: Robert M. Macnab, Keiichi Namba, Kelly T. Hughes, Nao Moriya, Tohru Minamino

Publikováno v: Journal of Molecular Biology. 359:466-477

Salmonella flagellar hook length is controlled at the level of export substrate specificity of the FlhB component of the type III flagellar export apparatus. FliK is believed to be the hook length sensor and interacts with FlhB to change its export s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::354539dbd52b4dfa6d1946c5fbf573ea
https://doi.org/10.1016/j.jmb.2006.03.025

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Crystallization and preliminary X-ray analysis of the C-terminal cytoplasmic domain of FlhA, a membrane-protein subunit of the bacterial flagellar type III protein-export apparatus

Autor: Katsumi Imada, Robert M. Macnab, May Kihara, Keiichi Namba, Yumiko Saijo-Hamano, Tohru Minamino

Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:599-602

The axial components of the bacterial flagellum and the scaffolding proteins for its assembly are exported through the flagellar-specific type III protein-export apparatus, which is believed to be located on the cytoplasmic surface of the basal body.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db2d123ce58a16a2737972b0f22b447c
https://doi.org/10.1107/s1744309105015745

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Structural and Functional Analysis of the C-terminal Cytoplasmic Domain of FlhA, an Integral Membrane Component of the Type III Flagellar Protein Export Apparatus in Salmonella

Autor: Yumiko Saijo-Hamano, Robert M. Macnab, Tohru Minamino, Keiichi Namba

Publikováno v: Journal of Molecular Biology. 343:457-466

FlhA is an integral membrane component of the Salmonella type III flagellar protein export apparatus. It consists of 692 amino acid residues and has two domains: the N-terminal transmembrane domain consisting of the first 327 amino acid residues, and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8df9e64f0a662bf0b7ce7dc05553a41a
https://doi.org/10.1016/j.jmb.2004.08.067

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Domain Organization and Function of Salmonella FliK, a Flagellar Hook-length Control Protein

Autor: Tohru Minamino, Yumiko Saijo-Hamano, Yukio Furukawa, Bertha González-Pedrajo, Robert M. Macnab, Keiichi Namba

Publikováno v: Journal of Molecular Biology. 341:491-502

Salmonella hook-length control protein FliK, which consists of 405 amino acid residues, switches substrate specificity of the type III flagellar protein export apparatus from rod/ hook-type to filament-type by causing a conformational change in the c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f2ddc54850fb042d18161171bb202a2
https://doi.org/10.1016/j.jmb.2004.06.012

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Analysis of an Engineered Salmonella Flagellar Fusion Protein, FliR-FlhB

Autor: Robert M. Macnab, May Kihara, Jonathan L. McMurry, John S. Van Arnam

Publikováno v: Journal of Bacteriology. 186:2495-2498

Salmonella FliR and FlhB are membrane proteins necessary for flagellar export. In Clostridium a fliR-flhB fusion gene exists. We constructed a similar Salmonella fusion gene which is able to complement fliR , flhB , and fliR flhB null strains. Wester

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https://doi.org/10.1128/jb.186.8.2495-2498.2004

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How Bacteria Assemble Flagella

Autor: Robert M. Macnab

Publikováno v: Annual Review of Microbiology. 57:77-100

▪ Abstract The bacterial flagellum is both a motor organelle and a protein export/assembly apparatus. It extends from the cytoplasm to the cell exterior. All the protein subunits of the external elements have to be exported. Export employs a type I

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https://doi.org/10.1146/annurev.micro.57.030502.090832

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The ATPase FliI Can Interact with the Type III Flagellar Protein Export Apparatus in the Absence of Its Regulator, FliH

Autor: May Kihara, Tohru Minamino, Keiichi Namba, Bertha González-Pedrajo, Robert M. Macnab

Publikováno v: Journal of Bacteriology. 185:3983-3988

Salmonella FliI is the ATPase that drives flagellar protein export. It normally exists as a complex together with the regulatory protein FliH. A fliH null mutant was slightly motile, with overproduction of FliI resulting in substantial improvement of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::196f9dcdd8157836028fec032ca6d05d
https://doi.org/10.1128/jb.185.13.3983-3988.2003

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