Structural Evidence That Colicin A Protein Binds to a Novel Binding Site of TolA Protein in Escherichia coli Periplasm

Li, Chan; Zhang, Ying; Vankemmelbeke, Mireille; Hecht, Oliver; Aleanizy, Fadilah Sfouq; Macdonald, Colin; Moore, Geoffrey R.; James, Richard; Penfold, Christopher N.

doi:10.1074/jbc.m112.342246

Cited by 18 publications

(25 citation statements)

References 64 publications

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“…Tol-dependent colicins have been shown to interact with one or more of the Tol proteins during their translocation across the periplasm, showing some similarities with Tol-dependent filamentous phage uptake. In 2012, Li et al (28) demonstrated that a colicin A peptide (residues 53-107) binds on the convex face of TolAIII Ec , forming an intermolecular antiparallel ␤-sheet.…”

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confidence: 99%

Electrostatic interactions between the CTX phage minor coat protein and the bacterial host receptor TolA drive the pathogenic conversion of Vibrio cholerae

Houot

Navarro²,

Nouailler

et al. 2017

Journal of Biological Chemistry

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is a natural inhabitant of aquatic environments and converts to a pathogen upon infection by a filamentous phage, CTXΦ, that transmits the cholera toxin-encoding genes. This toxigenic conversion of has evident implication in both genome plasticity and epidemic risk, but the early stages of the infection have not been thoroughly studied. CTXΦ transit across the bacterial periplasm requires binding between the minor coat protein named pIII and a bacterial inner-membrane receptor, TolA, which is part of the conserved Tol-Pal molecular motor. To gain insight into the TolA-pIII complex, we developed a bacterial two-hybrid approach, named Oxi-BTH, suited for studying the interactions between disulfide bond-folded proteins in the bacterial cytoplasm of an reporter strain. We found that two of the four disulfide bonds of pIII are required for its interaction with TolA. By combining Oxi-BTH assays, NMR, and genetic studies, we also demonstrate that two intermolecular salt bridges between TolA and pIII provide the driving forces of the complex interaction. Moreover, we show that TolA residue Arg-325 involved in one of the two salt bridges is critical for proper functioning of the Tol-Pal system. Our results imply that to prevent host evasion, CTXΦ uses an infection strategy that targets a highly conserved protein of Gram-negative bacteria essential for the fitness of in its natural environment.

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confidence: 99%

Electrostatic interactions between the CTX phage minor coat protein and the bacterial host receptor TolA drive the pathogenic conversion of Vibrio cholerae

Houot

Navarro²,

Nouailler

et al. 2017

Journal of Biological Chemistry

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“…X-ray structures of ColB [25] and ColM [26] show something similar with their TonB epitopes interacting with structured regions of the same molecule and other N-terminal residues being more flexible. NMR reveals that the TolB epitope of ColA binds intramolecularly to a globular domain of the protein in solution [27], but the TolB epitope of ColE9 behaves differently [17,28]. The two tryptophan residues in its TolB epitope promote the formation of clusters [17,20] of interacting residues (Figure 2), which then interact with each other instead of with a globular domain of the colicin [17].…”

Section: The T-domains (Translocation Domains) Of Colicins Contain Lomentioning

confidence: 99%

Intrinsically disordered proteins: lessons from colicins

Hecht

Macdonald

Moore

2012

Biochemical Society Transactions

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Defining structural features of IDPs (intrinsically disordered proteins) and relating these to biological function requires characterization of their dynamical properties. In the present paper, we review what is known about the IDPs of colicins, protein antibiotics that use their IDPs to enter bacterial cells. The structurally characterized colicin IDPs we consider contain linear binding epitopes for proteins within their target cells that the colicin hijacks during entry. We show that these binding epitopes take part in intramolecular interactions in the absence of protein partners, i.e. self-recognition, and consider the structural origins of this and its functional implications. We suggest that self-recognition is common in other IDPs that contain similar types of binding epitopes.

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“…The function of TolA is not fully understood, it is involved in the structural integrity of E. coli and related bacterial cell membranes. It is also involved in active transport across the membrane but can be parasitized by colicins produced by other E. coli resulting in the death of the cell (Li et al 2012). The Tol system also allows uptake of phage DNA, although generally deleterious imported DNA may contain genes that could give the cell an advantage.…”

Section: Discussionmentioning

confidence: 99%

In Silico Resurrection of the Major Vault Protein Suggests It Is Ancestral in Modern Eukaryotes

Daly

Sutherland-Smith

Penny

2013

Genome Biology and Evolution

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Vaults are very large oligomeric ribonucleoproteins conserved among a variety of species. The rat vault 3D structure shows an ovoid oligomeric particle, consisting of 78 major vault protein monomers, each of approximately 861 amino acids. Vaults are probably the largest ribonucleoprotein structures in eukaryote cells, being approximately 70 nm in length with a diameter of 40 nm—the size of three ribosomes and with a lumen capacity of 50 million Å3. We use both protein sequences and inferred ancestral sequences for in silico virtual resurrection of tertiary and quaternary structures to search for vaults in a wide variety of eukaryotes. We find that the vault’s phylogenetic distribution is widespread in eukaryotes, but is apparently absent in some notable model organisms. Our conclusion from the distribution of vaults is that they were present in the last eukaryote common ancestor but they have apparently been lost from a number of groups including fungi, insects, and probably plants. Our approach of inferring ancestral 3D and quaternary structures is expected to be useful generally.

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Structural Evidence That Colicin A Protein Binds to a Novel Binding Site of TolA Protein in Escherichia coli Periplasm

Cited by 18 publications

References 64 publications

Electrostatic interactions between the CTX phage minor coat protein and the bacterial host receptor TolA drive the pathogenic conversion of Vibrio cholerae

Electrostatic interactions between the CTX phage minor coat protein and the bacterial host receptor TolA drive the pathogenic conversion of Vibrio cholerae

Intrinsically disordered proteins: lessons from colicins

In Silico Resurrection of the Major Vault Protein Suggests It Is Ancestral in Modern Eukaryotes

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