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Article

Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus.

Journal of bacteriology - 1 Feb 2013

Ibuki Tatsuya, Uchida Yumiko, Hironaka Yusuke, Namba Keiichi, Imada Katsumi, Minamino Tohru

Abstract excerpt

A soluble protein, FliJ, along with a membrane protein, FlhA, plays a role in the energy coupling mechanism for bacterial flagellar protein export. The water-soluble FliH(X)-FliI(6) ATPase ring complex allows FliJ to efficiently interact with FlhA. However, the FlhA binding site of FliJ remains unknown. Here, we carried out genetic analysis of a region formed by well-conserved residues-Gln38, Leu42, Tyr45, Tyr49,...

Topics

Bacterial Proteins
Biological Transport
Escherichia coli
Gene Expression Regulation, Bacterial
Membrane Proteins
Models, Molecular
Mutation
Plasmids
Protein Binding
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Salmonella enterica

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Identifiers

PMID: 23161028
DOI: 10.1128/JB.01711-12
PMCID: PMC3554004

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