Robert M. Macnab

article

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

Nao Moriya, Tohru Minamino, Kelly T. Hughes, Robert M. Macnab, more

Journal of Molecular Biology > 2006 > 359 > 2 > 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 specificity upon hook completion. To find properties of FliK expected of such a molecular ruler, we assayed binding of FliK to the hook and found that...

article

Type III flagellar protein export and flagellar assembly

Robert M. Macnab

BBA - Molecular Cell Research > 2004 > 1694 > 1-3 > 207-217

Bacterial flagella, unlike eukaryotic flagella, are largely external to the cell and therefore many of their subunits have to be exported. Export is ATP-driven. In Salmonella, the bacterium on which this chapter largely focuses, the apparatus responsible for flagellar protein export consists of six membrane components, three soluble components and several substrate-specific chaperones. Other flagellated...

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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

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

Journal of Molecular Biology > 2004 > 343 > 2 > 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 the C-terminal cytoplasmic domain (FlhA _C ) comprising the remainder. Here, we have investigated the structure and function of FlhA _C ...

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

Tohru Minamino, Yumiko Saijo-Hamano, Yukio Furukawa, Bertha González-Pedrajo, more

Journal of Molecular Biology > 2004 > 341 > 2 > 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 cytoplasmic domain of FlhB (FlhB_C) upon completion of the hook assembly. An N-terminal region of FliK contains an export signal, and a highly conserved...

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Structural Properties of FliH, an ATPase Regulatory Component of the Salmonella Type III Flagellar Export Apparatus

Tohru Minamino, Bertha González-Pedrajo, Kenji Oosawa, Keiichi Namba, more

Journal of Molecular Biology > 2002 > 322 > 2 > 281-290

FliH is a regulatory component for FliI, the ATPase that is responsible for driving flagellar protein export in Salmonella. FliH consists of 235 amino acid residues, has a quite elongated shape, exists as a homodimer and together with FliI forms a heterotrimer. Here, we have investigated the structural properties of the FliH homodimer in further detail. Like intact His-tagged FliH homodimer, fragment...

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Interactions among Membrane and Soluble Components of the Flagellar Export Apparatus of Salmonella ^†

Keng Zhu, Bertha González-Pedrajo, Robert M. Macnab

Biochemistry > 2002 > 41 > 30 > 9516 - 9524

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Proteolytic analysis of the FliH/FliI complex, the ATPase component of the type III flagellar export apparatus of Salmonella1 1 Edited by M. F. Moody

Tohru Minamino, Jeremy R.H Tame, Keiichi Namba, Robert M Macnab

Journal of Molecular Biology > 2001 > 312 > 5 > 1027-1036

The ATPase FliI of the Salmonella type III flagellar protein export apparatus is a 456 amino acid residue cytoplasmic protein consisting of two regions, an N-terminal flagellum-specific region and a C-terminal ATPase region. It forms a complex with a regulatory protein FliH in the cytoplasm. Multi-angle light-scattering studies indicate that FliH forms a homodimer, (FliH)₂, and that FliH and FliI...

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The role in flagellar rod assembly of the N-terminal domain of Salmonella FlgJ, a flagellum-specific muramidase

Takanori Hirano, Tohru Minamino, Robert M. Macnab

Journal of Molecular Biology > 2001 > 312 > 2 > 359-369

The C-terminal half of the Salmonella flagellar protein FlgJ has peptidoglycan hydrolyzing activity and it has been suggested that it is a flagellum-specific muramidase which locally digests the peptidoglycan layer to permit assembly of the rod structure to proceed through the periplasmic space. It was also suggested that FlgJ might be involved in rod formation itself, although there was no direct...

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Effect of cellular level of fliK on flagellar hook and filament assembly in Salmonella typhimurium11Edited by M. F. Moody

Kazumasa Muramoto, Shigeru Makishima, Shin-Ichi Aizawa, Robert M Macnab

Journal of Molecular Biology > 1998 > 277 > 4 > 871-882

Frameshift mutations in the fliK gene of Salmonella result in abnormal elongation of the hook and the failure to assemble filament (polyhook phenotype). Second-site suppressor mutations restore filament assembly, but the cells often remain defective in hook-length control (polyhook-filament phenotype). Where the suppressor mutations are intragenic, the second mutation restores the original frame,...

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Distinct regions of bacterial flagellar switch protein FliM interact with FliG, FliN and CheY11Edited by M. F. Moody

Anne S Toker, Robert M Macnab

Journal of Molecular Biology > 1997 > 273 > 3 > 623-634

The FliG, FliM, and FliN proteins of the bacterial flagellar motor are believed to interact with one another to form the switch complex, which in turn is thought to interact with one of the chemotaxis proteins, CheY. In particular, FliM appears to be an intermediary between CheY and FliG: the current model suggests that CheY, when phosphorylated (CheY-P), binds to FliM and produces a conformational...

article

Running tests on a miniature motor

Robert M. Macnab

Biophysical Journal > 1993 > 64 > 3 > 934-935

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Search results for: Robert M. Macnab

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

Type III flagellar protein export and flagellar assembly

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

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

Structural Properties of FliH, an ATPase Regulatory Component of the Salmonella Type III Flagellar Export Apparatus

Interactions among Membrane and Soluble Components of the Flagellar Export Apparatus of Salmonella ^†

Proteolytic analysis of the FliH/FliI complex, the ATPase component of the type III flagellar export apparatus of Salmonella1 1 Edited by M. F. Moody

The role in flagellar rod assembly of the N-terminal domain of Salmonella FlgJ, a flagellum-specific muramidase

Effect of cellular level of fliK on flagellar hook and filament assembly in Salmonella typhimurium11Edited by M. F. Moody

Distinct regions of bacterial flagellar switch protein FliM interact with FliG, FliN and CheY11Edited by M. F. Moody

Running tests on a miniature motor

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