Abstract
In certain bacterial mutants, called groE, T4 phage head assembly is blocked specifically, implying that the host plays a direct role in head assembly. The block occurs early in the assembly process at the level of action of T4 gene 31.
This is a preview of subscription content, access via your institution
Access options
Similar content being viewed by others
References
Levine, M., Ann. Rev. Genetics, 3, 323 (1969).
Eiserling, F. A., & Dickson, R. C., Ann. Rev. Biochem. (in the press).
Edgar, R. S., & Wood, W. B., Proc. US Nat. Acad. Sci., 55, 498 (1966).
Edgar, R. S., & Lielausis, I., J. Mol. Biol., 32, 263 (1968).
Georgopoulos, C. P., Proc. US Nat. Acad. Sci., 68, 2977 (1971).
Georgopoulos, C. P., & Herskowitz, I., in The Bacteriophage Lambda (edit. by Hershey, A.), 553 (Cold Spring Harbor Laboratory, New York, 1971).
Philipson, L., Albertson, P. A., & Frick, G., Virology, 11, 553 (1960).
Laemmli, U. K., Nature, 227, 680 (1970).
Dickson, R. C., Barnes, S. L., & Eiserling, F. A., J. Mol. Biol., 53, 461 (1970).
Hosoda, J., & Cone, R., Proc. US Nat. Acad. Sci., 66, 1275 (1970).
Kellenberger, E., & Kellenberger-Van Der Kamp, E., FEBS Lett., 8, 3, 140 (1970).
Laemmli, U. K., Beguin, F., & Gujer-Kellenberger, B., J. Mol. Biol., 47, 69 (1969).
Kellenberger, E., in Principles of Biomolecular Organization, Ciba Foundation Symp. (Churchill, London, 1966).
Reid, M. S., & Bielski, R. L., Anal. Biochem., 21, 374 (1968).
Fairbanks, G., Levinthal, C., & Reeder, R. H., Biochem. Biophys. Res. Commun., 20, 393 (1965).
Sonenshein, A. L., & Roscoe, D. H., Virology, 39, 265 (1969).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
GEORGOPOULOS, C., HENDRIX, R., KAISER, A. et al. Role of the Host Cell in Bacteriophage Morphogenesis: Effects of a Bacterial Mutation on T4 Head Assembly. Nature New Biology 239, 38–41 (1972). https://doi.org/10.1038/newbio239038a0
Received:
Revised:
Issue date:
DOI: https://doi.org/10.1038/newbio239038a0
This article is cited by
-
The versatile mutational “repertoire” of Escherichia coli GroEL, a multidomain chaperonin nanomachine
Biophysical Reviews (2018)
-
Novel chaperonins are prevalent in the virioplankton and demonstrate links to viral biology and ecology
The ISME Journal (2017)
-
Protein folding in the cell: an inside story
Nature Medicine (2011)
-
The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding
Nature Structural Biology (1998)
-
Heat induced stress proteins and the concept of molecular chaperones
Journal of Biosciences (1998)
