The Baseplate Wedges of Bacteriophage T4 Spontaneously Assemble into Hubless Baseplate-Like Structure In Vitro

Yap, Moh Lan; Mio, Kazuhiro; Leiman, P.G.; Kanamaru, Shuji; Arisaka, Fumio

doi:10.1016/j.jmb.2009.10.071

Cited by 28 publications

(54 citation statements)

References 23 publications

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“…T4 gp53, added to the wedge after gp6, is a unique component of the T4 baseplate but does bear a LysM-like domain, which may play a similar role to LysM domains in simple baseplates. Complete T4 wedges assemble into a hexameric "star" conformation similar to the baseplate conformation observed in the contracted tail (13). In contrast, the Mu baseplate wedges did not assemble into stable ring-like structures in the absence of the hub proteins.…”

Section: Discussionmentioning

confidence: 66%

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Baseplate assembly of phage Mu: Defining the conserved core components of contractile-tailed phages and related bacterial systems

Buttner

Maxwell

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Contractile phage tails are powerful cell puncturing nanomachines that have been co-opted by bacteria for self-defense against both bacteria and eukaryotic cells. The tail of phage T4 has long served as the paradigm for understanding contractile tail-like systems despite its greater complexity compared with other contractile-tailed phages. Here, we present a detailed investigation of the assembly of a "simple" contractile-tailed phage baseplate, that of Escherichia coli phage Mu. By coexpressing various combinations of putative Mu baseplate proteins, we defined the required components of this baseplate and delineated its assembly pathway. We show that the Mu baseplate is constructed through the independent assembly of wedges that are organized around a central hub complex. The Mu wedges are comprised of only three protein subunits rather than the seven found in the equivalent structure in T4. Through extensive bioinformatic analyses, we found that homologs of the essential components of the Mu baseplate can be identified in the majority of contractile-tailed phages and prophages. No T4-like prophages were identified. The conserved simple baseplate components were also found in contractile tailderived bacterial apparatuses, such as type VI secretion systems, Photorhabdus virulence cassettes, and R-type tailocins. Our work highlights the evolutionary connections and similarities in the biochemical behavior of phage Mu wedge components and the TssF and TssG proteins of the type VI secretion system. In addition, we demonstrate the importance of the Mu baseplate as a model system for understanding bacterial phage tail-derived systems.baseplate | assembly | contractile tail | phage Mu

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Section: Discussionmentioning

confidence: 66%

“…3). The dimeric nature of the Mu baseplate wedge contrasts with the T4 wedge, which contains subunits ranging in number from one to three and does not form a dimer before interaction with the hub complex (13).…”

Section: Resultsmentioning

confidence: 96%

Baseplate assembly of phage Mu: Defining the conserved core components of contractile-tailed phages and related bacterial systems

Buttner

Maxwell

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…It is particularly useful for quantitatively charactering the solution behavior such as self-or hetero-association of biomolecules (31)(32)(33)(34). SVA was used to prove the trimer formation of N36Fd and N28Fd peptides.…”

Section: Design Of N36fd and N28fdmentioning

confidence: 99%

“…However, multiple peaks appeared in the result of SVA of N36FdϩC34, suggesting that several species with different molecular shapes may exist in the mixture. In such cases, fitting data using the measured f/f 0 , the weight average of the frictional ratio of molecular species present in solution, may lead to considerable errors (34). A possible explanation for the deviation of the obtained molecular weights of the two major peaks of N36FdϩC34 from their calculated weights is the presence of multiple species, such as monomeric and dimeric 6-HB, in the solution.…”

Section: Interaction Of N36fd and N28fd Trimers With C34 Peptide Resumentioning

confidence: 99%

Novel Recombinant Engineered gp41 N-terminal Heptad Repeat Trimers and Their Potential as Anti-HIV-1 Therapeutics or Microbicides

Chen

et al. 2010

Journal of Biological Chemistry

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Peptides derived from N-terminal heptad repeat (NHR) of the HIV-1 gp41 are generally poor inhibitors of HIV-1 entry, because they tend to aggregate and do not form a trimeric coiled-coil. In this study, we have fused portions of gp41 NHR, e.g. N36 or N28, to the T4 fibritin trimerization domain, Foldon (Fd), thus constructing novel NHR trimers, designated N36Fd or N28Fd, which could be expressed in Escherichia coli cells. The purified N36Fd and N28Fd exhibited SDS-resistant trimeric coiled-coil conformation with improved ␣-helicity compared with the corresponding N-peptides. They could interact with a C-peptide (e.g. C34) to form stable six-helix bundle and possessed potent anti-HIV-1 activity against a broad spectrum of HIV-1 strains. N28Fd was effective against T20-resistant HIV-1 variants and more resistant to proteinase K compared with T20 (enfuvirtide), a C-peptide-based HIV fusion inhibitor. Therefore, N28Fd trimer has great potentials for further development as an affordable therapeutic or microbicide for treatment and prevention of HIV-1 infection.

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“…Genes were expressed separately and the cells which express different genes were first mixed and then lysed. For details of the experiments, see Yap et al (2010a). The results are shown in Table 2.…”

Section: Introductionmentioning

confidence: 99%

Protein interactions in the assembly of the tail of bacteriophage T4

Arisaka

Kanamaru

2013

Biophys Rev

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Protein interactions in the assembly of the baseplate have been investigated. The baseplate of the phage T4 tail consists of a hub and six wedges which surround the former. Both reversible and irreversible interactions were found. Reversible association includes gp5 and gp27 (gp: gene product) which form a complex in a pH-dependent manner and gp18 polymerization, i.e. the tail sheath formation depends on the ionic strength. These reversible interactions were followed by irreversible or tight binding which pulls the whole association reaction to complete the assembly. The wedge assembly is strictly ordered which means that if one of the seven wedge proteins is missing, the assembly proceeds to that point and the remaining molecules stay non-associated. The strictly sequential assembly pathway is suggested to be materialized by successive conformational change upon binding, which can be shown by proteolytic probe.

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The Baseplate Wedges of Bacteriophage T4 Spontaneously Assemble into Hubless Baseplate-Like Structure In Vitro

Cited by 28 publications

References 23 publications

Baseplate assembly of phage Mu: Defining the conserved core components of contractile-tailed phages and related bacterial systems

Baseplate assembly of phage Mu: Defining the conserved core components of contractile-tailed phages and related bacterial systems

Novel Recombinant Engineered gp41 N-terminal Heptad Repeat Trimers and Their Potential as Anti-HIV-1 Therapeutics or Microbicides

Protein interactions in the assembly of the tail of bacteriophage T4

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