TolA central domain interacts with Escherichia coli porins.

Derouiche, Rahmona; Gavioli, Marthe; Bénédetti, Hélène; Prilipov, Alexej; Lazdunski, Claude; Lloubès, Roland

doi:10.1002/j.1460-2075.1996.tb01032.x

Cited by 72 publications

(85 citation statements)

References 35 publications

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“…It was implied that once the N2 domain binds to the tip of the pilus, its affinity for the N1 domain decreases, leaving this part of g3p free to interact with its secondary receptor. After depolymerization of the pilus, the released N1 domain can interact with the CT part of TolA localized on the inside of the outer membrane (7,9,27). Our observation of a second F-pilus-interacting domain (L1) could reflect the fact that amino acid residues 68 to 86 of g3p might constitute the pilus-binding epitope together with residues in the N2 domain.…”

Section: Discussionmentioning

confidence: 77%

“…N2 mediates the interaction with the first bacterial receptor, the F pilus (1). The first domain (N1) is believed to interact with the second receptor, the TolQRA protein complex, spanning the periplasmic space and the inner membrane (5,9,27,31). It has previously been shown that phage with only the N1 and the CT domains on its surface will infect at a drastically reduced level.…”

Section: Discussionmentioning

confidence: 99%

“…Through the depolymerization of the pilus, the bacteriophage is brought close to the cell surface of the host, where the interaction with the coreceptor takes place (5,31). The coreceptor, i.e., the TolQRA complex, is localized in the inner membrane and the periplasmic space and is attached to the inside of the outer membrane (9,16). It was recently shown that it is the C-terminal part of the TolA domain that interacts with the bacteriophage adsorption protein (7,27).…”

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confidence: 99%

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The Phage Infection Process: a Functional Role for the Distal Linker Region of Bacteriophage Protein 3

Nilsson

Malmborg

Borrebaeck

2000

J Virol

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The filamentous bacteriophage infects Escherichia coli by interaction with the F pilus and the TolQRA complex. The virus-encoded protein initiating this process is the gene 3 protein (g3p). The g3p molecule can be divided into three different domains separated by two glycine-rich linker regions. Though there has been extensive evaluation of the importance of the diverse domains of g3p, no proper function has so far been assigned to these linker regions. Through the design of mutated variants of g3p that were displayed on the surface of bacteriophage, we were able to elucidate a possible role for the distal glycine-rich linker region. A phage that displayed a g3p comprised of only the N1 domain, the first linker region, and the C-terminal domain was able to infect cells at almost the same frequency as the wild-type phage. This infection was proven to be dependent on the motif between amino acid residues 68 and 86 (i.e., the first glycine-rich linker region of g3p) and on F-pilus expression.Filamentous bacteriophage is a nonlytic DNA virus that infects Escherichia coli cells harboring an F episome (19,20,26). In order for bacteriophage infection to occur, including the translocation of the single-stranded phage DNA over the cell membrane, the expression of two different receptor systems in the gram-negative host cell is critical. The primary receptor, i.e., the F pilus, mediates the adsorption of the phage to the bacterial cell (6,12). This interaction can take place at a long distance from the cell surface, since the pilus molecule extrudes away from the bacteria. Through the depolymerization of the pilus, the bacteriophage is brought close to the cell surface of the host, where the interaction with the coreceptor takes place (5, 31). The coreceptor, i.e., the TolQRA complex, is localized in the inner membrane and the periplasmic space and is attached to the inside of the outer membrane (9, 16). It was recently shown that it is the C-terminal part of the TolA domain that interacts with the bacteriophage adsorption protein (7,27). Upon binding to the TolA domain, the viral DNA translocates into the host cell by an as-yet-unknown mechanism.Expression of the gene 3 viral adsorption protein, g3p, on the surface of the bacteriophage is essential for normal infection to occur (1). The minor coat protein g3p is located together with g6p in three to five copies at one end of the filamentous phage (10). Mature g3p consists of 406 amino acid residues separated in several distinct regions (2). The N-terminal part can be divided into two different domains, N1 and N2, mediating penetration and adsorption during infection, respectively (1, 30). The C-terminal part is responsible for the interaction with g6p, thereby anchoring the g3p in the membrane of the phage coat (1, 14, 21). Furthermore, the g3p has a crucial role in the assembly of the filamentous phage, since in the absence of g3p, the proper termination of the assembly and the following release of the phage will not take place (24).Two glycine-rich linker regions divid...

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Section: Discussionmentioning

confidence: 77%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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The Phage Infection Process: a Functional Role for the Distal Linker Region of Bacteriophage Protein 3

Nilsson

Malmborg

Borrebaeck

2000

J Virol

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“…Because the exact function is not known, current research focuses on the link between Tol-Pal proteins and porins, lipopolysaccharides (LPS), or O-antigen biogenesis. It has been shown that the central domain of the TolA protein, as well as the TolB protein, interacts in vitro with major OM trimeric porins such as OmpF, OmpC, LamB, and PhoE in the presence of sodium dodecyl sulfate (150,554). TolA and TolB do not interact with OmpA or the OM denaturated porins.…”

Section: Tol-dependent Colicinsmentioning

confidence: 99%

Colicin Biology

Cascales

Buchanan

Duché

et al. 2007

Microbiol Mol Biol Rev

969

1,324

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SUMMARY Colicins are proteins produced by and toxic for some strains of Escherichia coli. They are produced by strains of E. coli carrying a colicinogenic plasmid that bears the genetic determinants for colicin synthesis, immunity, and release. Insights gained into each fundamental aspect of their biology are presented: their synthesis, which is under SOS regulation; their release into the extracellular medium, which involves the colicin lysis protein; and their uptake mechanisms and modes of action. Colicins are organized into three domains, each one involved in a different step of the process of killing sensitive bacteria. The structures of some colicins are known at the atomic level and are discussed. Colicins exert their lethal action by first binding to specific receptors, which are outer membrane proteins used for the entry of specific nutrients. They are then translocated through the outer membrane and transit through the periplasm by either the Tol or the TonB system. The components of each system are known, and their implication in the functioning of the system is described. Colicins then reach their lethal target and act either by forming a voltage-dependent channel into the inner membrane or by using their endonuclease activity on DNA, rRNA, or tRNA. The mechanisms of inhibition by specific and cognate immunity proteins are presented. Finally, the use of colicins as laboratory or biotechnological tools and their mode of evolution are discussed.

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“…This role is probably important, as homologs of the Tol proteins are found in several gram-negative bacteria, including Haemophilus influenzae (7), Brucella abortus (22), Pseudomonas putida (21), and Pseudomonas aeruginosa (18). The central domain of TolA specifically interacts with trimeric porins such as OmpC, OmpF, LamB, and PhoE (9). Such interactions have been proposed to be involved in the process of assembly of outer membrane trimeric porins and to be relevant to the function of the Tol system.…”

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confidence: 99%

The TolB protein interacts with the porins of Escherichia coli

et al. 1997

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TolB is a periplasmic protein of the cell envelope Tol complex. It is partially membrane associated through an interaction with the outer membrane lipoprotein PAL (peptidoglycan-associated lipoprotein), which also belongs to the Tol system. The interaction of TolB with outer membrane porins of Escherichia coli was investigated with a purified TolB derivative harboring a six-histidine tag. TolB interacted with the trimeric porins OmpF, OmpC, PhoE, and LamB but not with their denatured monomeric forms or OmpA. These interactions took place both in the presence and in the absence of lipopolysaccharide. TolA, an inner membrane component of the Tol system, also interacts with the trimeric porins via its central periplasmic domain (R. Dérouiche, M. Gavioli, H. Bénédetti, A. Prilipov, C. Lazdunski, and R. Lloubès, EMBO J. 15:6408-6415, 1996). In the presence of the purified central domain of TolA (TolAIIHis), the TolB-porin complexes disappeared to form TolAIIHis-porin complexes. These results suggest that the interactions of TolA and TolB with porins might take place in vivo and might be concomitant events participating in porin assembly. They also suggest that the Tol system as a whole may be involved in porin assembly in the outer membrane.

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TolA central domain interacts with Escherichia coli porins.

Cited by 72 publications

References 35 publications

The Phage Infection Process: a Functional Role for the Distal Linker Region of Bacteriophage Protein 3

The Phage Infection Process: a Functional Role for the Distal Linker Region of Bacteriophage Protein 3

Colicin Biology

The TolB protein interacts with the porins of Escherichia coli

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