Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2013 Jun;5(2):79-84.
doi: 10.1007/s12551-013-0114-2. Epub 2013 Apr 24.

Protein interactions in the assembly of the tail of bacteriophage T4

Affiliations
Review

Protein interactions in the assembly of the tail of bacteriophage T4

Fumio Arisaka et al. Biophys Rev. 2013 Jun.

Abstract

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.

Keywords: Analytical ultracentrifugation; Bacteriophage; Contractile tail; Protein assembly; Protein interaction; Reversible association.

PubMed Disclaimer

Figures

Fig. 1
Fig. 1
Sedimentation equilibrium of gp27–gp5* complex at pH 6 and pH 8

References

    1. Abuladze NK, Gingery M, Tsai J, Eiserling FA. Tail length determination in bacteriophage T4. Virology. 1994;199:301–310. doi: 10.1006/viro.1994.1128. - DOI - PubMed
    1. Aksyuk AA, Leiman PG, Kurochkina LP, Shneider MM, Kostyuchenko VA, Mesyanzhinov VV, Rossmann MG. The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria. EMBO J. 2009;28:821–829. doi: 10.1038/emboj.2009.36. - DOI - PMC - PubMed
    1. Arisaka F, Tschopp J, van Driel R, Engel J. Reassembly of the bacteriophage T4 tail from the core­baseplate and the monomeric sheath protein P18: a cooperative association process. J Mol Biol. 1979;132:369–386. doi: 10.1016/0022-2836(79)90266-3. - DOI - PubMed
    1. Epstein RH, Bolle A, Steinberg C, Kellenberger E, Boy de la Tour E, Chevalley R, Edgar R, Susman M, Denhart C, Lielausis I. Physiological studies of conditional lethal mutants of bacteriophage T4D. Cold Spring Harb Symp Quant Biol. 1964;28:375–392. doi: 10.1101/SQB.1963.028.01.053. - DOI
    1. Ferguson PL, Coombs DH. Pulse-chase analysis of the in vivo assembly of the bacteriophage T4 tail. J Mol Biol. 2000;297:99–117. doi: 10.1006/jmbi.2000.3551. - DOI - PubMed

LinkOut - more resources