The FlhA linker mediates flagellar protein export switching during flagellar assembly. 2021

Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.

The flagellar protein export apparatus switches substrate specificity from hook-type to filament-type upon hook assembly completion, thereby initiating filament assembly at the hook tip. The C-terminal cytoplasmic domain of FlhA (FlhAC) serves as a docking platform for flagellar chaperones in complex with their cognate filament-type substrates. Interactions of the flexible linker of FlhA (FlhAL) with its nearest FlhAC subunit in the FlhAC ring is required for the substrate specificity switching. To address how FlhAL brings the order to flagellar assembly, we analyzed the flhA(E351A/W354A/D356A) ΔflgM mutant and found that this triple mutation in FlhAL increased the secretion level of hook protein by 5-fold, thereby increasing hook length. The crystal structure of FlhAC(E351A/D356A) showed that FlhAL bound to the chaperone-binding site of its neighboring subunit. We propose that the interaction of FlhAL with the chaperon-binding site of FlhAC suppresses filament-type protein export and facilitates hook-type protein export during hook assembly.

UI MeSH Term Description Entries
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D005407 Flagella A whiplike motility appendage present on the surface cells. Prokaryote flagella are composed of a protein called FLAGELLIN. Bacteria can have a single flagellum, a tuft at one pole, or multiple flagella covering the entire surface. In eukaryotes, flagella are threadlike protoplasmic extensions used to propel flagellates and sperm. Flagella have the same basic structure as CILIA but are longer in proportion to the cell bearing them and present in much smaller numbers. (From King & Stansfield, A Dictionary of Genetics, 4th ed) Flagellum
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D018832 Molecular Chaperones A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures. Chaperones, Molecular,Chaperone, Molecular,Molecular Chaperone
D019779 Salmonella enterica A subgenus of Salmonella containing several medically important serotypes. The habitat for the majority of strains is warm-blooded animals.
D021381 Protein Transport The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport. Cellular Protein Targeting,Gated Protein Transport,Protein Targeting, Cellular,Protein Translocation,Transmembrane Protein Transport,Vesicular Protein Transport,Protein Localization Processes, Cellular,Protein Sorting,Protein Trafficking,Protein Transport, Gated,Protein Transport, Transmembrane,Protein Transport, Vesicular,Traffickings, Protein

Related Publications

Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
November 2004, Biochimica et biophysica acta,
Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
April 2016, Molecular microbiology,
Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
March 2024, Communications biology,
Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
January 2011, PloS one,
Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
April 2010, Molecular microbiology,
Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
April 2018, Science advances,
Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
April 2010, Journal of bacteriology,
Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
February 2013, Journal of bacteriology,
Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
February 2012, Journal of molecular biology,
Yumi Inoue, and Miki Kinoshita, and Mamoru Kida, and Norihiro Takekawa, and Keiichi Namba, and Katsumi Imada, and Tohru Minamino
November 2008, Molecular bioSystems,
Copied contents to your clipboard!