Investigating the role of BN-domains of FlhF involved in flagellar synthesis in Campylobacter jejuni

Microbiol Res. 2022 Mar:256:126944. doi: 10.1016/j.micres.2021.126944. Epub 2021 Dec 14.

Abstract

FlhF protein is critical for intact flagellar assembly in Campylobacter jejuni. It is a putative GTPase with B-, N- and G-domains. However, the role of the B- and N-domains in flagella biosynthesis remains unclear in C. jejuni. This study demonstrated that both the B- and N-domains are essential for flagellar synthesis, with the absence of B- and/or N-domains showing truncated variants of FlhF by TEM. Point mutations in the B- and N-domains (T13A, K159A, G231A) also induced flagella abnormalities. Furthermore, significant defects in GTPase activity and polar targeting of FlhF were triggered by point mutations of B- and N-domains. Flagella gene expression and transcription were also significantly disrupted in flhF(T13A), flhF(K159A) and flhF(G231A) strains. This study initially explored the effects of B- and N-domains on flagella synthesis. We speculated that B- and N-domains may directly or indirectly cause flagella abnormalities by affecting flagellar gene expression or GTPase activity, which helps us better understand the function of FlhF in flagella synthesis.

Keywords: B-domain; Campylobacter jejuni; FlhF; N-domain; flagellar synthesis.

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Campylobacter jejuni* / genetics
  • Campylobacter jejuni* / metabolism
  • Flagella / genetics
  • Flagella / metabolism
  • Monomeric GTP-Binding Proteins* / genetics
  • Monomeric GTP-Binding Proteins* / metabolism
  • Point Mutation

Substances

  • Bacterial Proteins
  • Monomeric GTP-Binding Proteins