Correction: Kinetic and catalytic properties of M.HpyAXVII, a phase-variable DNA methyltransferase from Helicobacter pylori.

Prasad, Yedu; Kumar, Ritesh; Chaudhary, Awanish Kumar; Dhanaraju, Rajkumar; Majumdar, Soneya; Rao, Desirazu N.

doi:10.1074/jbc.aac119.010443

Journal of Biological Chemistry

2019

DOI: 10.1074/jbc.aac119.010443

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Correction: Kinetic and catalytic properties of M.HpyAXVII, a phase-variable DNA methyltransferase from Helicobacter pylori.

Yedu Prasad¹,

Ritesh Kumar²,

Awanish Kumar Chaudhary³

et al.

Abstract: There was an error in Fig. S3A. While compiling data from a doctoral thesis, the wrong image and quantification from a similar experiment was incorporated into the article. This error has now been corrected and does not affect the results or conclusions of the work. The authors apologize for the error.

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Control of the flagellation pattern in Helicobacter pylori by FlhF and FlhG

Gibson,

Botting,

Al-Otaibi

et al. 2023

J Bacteriol

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FlhF and FlhG control the location and number of flagella, respectively, in many polar-flagellated bacteria. The roles of FlhF and FlhG are not well characterized in bacteria that have multiple polar flagella, such as Helicobacter pylori . Deleting flhG in H. pylori shifted the flagellation pattern where most cells had approximately four flagella to a wider and more even distribution in flagellar number. As reported in other bacteria, deleting flhF in H. pylori resulted in reduced motility, hypoflagellation, and the improper localization of flagella to nonpolar sites. Motile variants of H. pylori ∆ flhF mutants that had a higher proportion of flagella localizing correctly to the cell pole were isolated, but we were unable to identify the genetic determinants responsible for the increased localization of flagella to the cell pole. One motile variant though produced more flagella than the Δ flhF parental strain, which apparently resulted from a missense mutation in fliF (encodes the MS ring protein), which changed Asn-255 to aspartate. Recombinant FliF N255D , but not recombinant wild-type FliF, formed ordered ring-like assemblies in vitro that were ~50 nm wide and displayed the MS ring architecture. We infer from these findings that the FliF N225D variant forms the MS ring more effectively in vivo in the absence of FlhF than wild-type FliF. IMPORTANCE Helicobacter pylori colonizes the human stomach where it can cause a variety of diseases, including peptic ulcer disease and gastric cancer. H. pylori uses flagella for motility, which is required for host colonization. FlhG and FlhF control the flagellation patterns in many bacteria. We found that in H. pylori , FlhG ensures that cells have approximately equal number of flagella and FlhF is needed for flagellum assembly and localization. FlhF is proposed to facilitate the assembly of FliF into the MS ring, which is one of the earliest structures formed in flagellum assembly. We identified a FliF variant that assembles the MS ring in the absence of FlhF, which supports the proposed role of FlhF in facilitating MS ring assembly.

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Control of the flagellation pattern in Helicobacter pylori by FlhF and FlhG

Gibson,

Botting,

Al-Otaibi

et al. 2023

J Bacteriol

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show abstract

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Correction: Kinetic and catalytic properties of M.HpyAXVII, a phase-variable DNA methyltransferase from Helicobacter pylori.

Cited by 1 publication

References 0 publications

Control of the flagellation pattern in Helicobacter pylori by FlhF and FlhG

Control of the flagellation pattern in Helicobacter pylori by FlhF and FlhG

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