Literature DB >> 36151384

Structure and Assembly of the Bacterial Flagellum.

Natalie S Al-Otaibi1, Julien R C Bergeron2.   

Abstract

The bacterial flagellum is a large macromolecular assembly that acts as propeller, providing motility through the rotation of a long extracellular filament. It is composed of over 20 different proteins, many of them highly oligomeric. Accordingly, it has attracted a huge amount of interest amongst researchers and the wider public alike. Nonetheless, most of its molecular details had long remained elusive.This however has changed recently, with the emergence of cryo-EM to determine the structure of protein assemblies at near-atomic resolution. Within a few years, the atomic details of most of the flagellar components have been elucidated, revealing not only its overall architecture but also the molecular details of its rotation mechanism. However, many questions remained unaddressed, notably on the complexity of the assembly of such an intricate machinery.In this chapter, we review the current state of our understanding of the bacterial flagellum structure, focusing on the recent development from cryo-EM. We also highlight the various elements that still remain to be fully characterized. Finally, we summarize the existing model for flagellum assembly and discuss some of the outstanding questions that are still pending in our understanding of the diversity of assembly pathways.
© 2022. The Author(s), under exclusive license to Springer Nature Switzerland AG.

Entities:  

Keywords:  Bacterial motility; Bacterial secretion systems; Cryo-EM; Macromolecular structure; Membrane proteins

Mesh:

Substances:

Year:  2022        PMID: 36151384     DOI: 10.1007/978-3-031-00793-4_13

Source DB:  PubMed          Journal:  Subcell Biochem        ISSN: 0306-0225


  82 in total

1.  Tetrameric structure of the flagellar cap protein FliD from Serratia marcescens.

Authors:  So Yeon Cho; Wan Seok Song; Ho Jeong Hong; Geun-Shik Lee; Seung Goo Kang; Hyun-Jeong Ko; Pyeung-Hyeun Kim; Sung-Il Yoon
Journal:  Biochem Biophys Res Commun       Date:  2017-05-18       Impact factor: 3.575

2.  Mystery of fliK in length control of the flagellar hook.

Authors:  Shin-Ichi Aizawa
Journal:  J Bacteriol       Date:  2012-07-13       Impact factor: 3.490

3.  Rebuttal: flagellar hook length is controlled by a secreted molecular ruler.

Authors:  Shin-Ichi Aizawa
Journal:  J Bacteriol       Date:  2012-07-13       Impact factor: 3.490

4.  Molecular characterization of the flagellar hook in Bacillus subtilis.

Authors:  Colleen R Courtney; Loralyn M Cozy; Daniel B Kearns
Journal:  J Bacteriol       Date:  2012-06-22       Impact factor: 3.490

5.  Rod-to-hook transition for extracellular flagellum assembly is catalyzed by the L-ring-dependent rod scaffold removal.

Authors:  Eli J Cohen; Kelly T Hughes
Journal:  J Bacteriol       Date:  2014-04-18       Impact factor: 3.490

6.  Dynamic properties of bacterial flagellar motors.

Authors:  H C Berg
Journal:  Nature       Date:  1974-05-03       Impact factor: 49.962

7.  Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima.

Authors:  Perry N Brown; Michael A A Mathews; Lisa A Joss; Christopher P Hill; David F Blair
Journal:  J Bacteriol       Date:  2005-04       Impact factor: 3.490

8.  Identification of the docking site between a type III secretion system ATPase and a chaperone for effector cargo.

Authors:  Sarah E Allison; Brian R Tuinema; Ellen S Everson; Seiji Sugiman-Marangos; Kun Zhang; Murray S Junop; Brian K Coombes
Journal:  J Biol Chem       Date:  2014-07-17       Impact factor: 5.157

9.  Structural modeling of the flagellum MS ring protein FliF reveals similarities to the type III secretion system and sporulation complex.

Authors:  Julien R Bergeron
Journal:  PeerJ       Date:  2016-02-22       Impact factor: 2.984

10.  The cryo-EM structure of the bacterial flagellum cap complex suggests a molecular mechanism for filament elongation.

Authors:  Natalie S Al-Otaibi; Aidan J Taylor; Daniel P Farrell; Svetomir B Tzokov; Frank DiMaio; David J Kelly; Julien R C Bergeron
Journal:  Nat Commun       Date:  2020-06-25       Impact factor: 14.919

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