P15 and P3, the Tail Completion Proteins of Bacteriophage T4, Both Form Hexameric Rings

Author:

Zhao Li1,Kanamaru Shuji2,Chaidirek Chatree'chalerm1,Arisaka Fumio1

Affiliation:

1. Department of Molecular and Cellular Assembly, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8501, Japan

2. Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-2054

Abstract

ABSTRACT Two proteins, gp15 and gp3 (gp for gene product), are required to complete the assembly of the T4 tail. gp15 forms the connector which enables the tail to bind to the head, whereas gp3 is involved in terminating the elongation of the tail tube. In this work, genes 15 and 3 were cloned and overexpressed, and the purified gene products were studied by analytical ultracentrifugation, electron microscopy, and circular dichroism. Determination of oligomerization state by sedimentation equilibrium revealed that both gp15 and gp3 are hexamers of the respective polypeptide chains. Electron microscopy of the negatively stained P15 and P3 (P denotes the oligomeric state of the gene product) revealed that both proteins form hexameric rings, the diameter of which is close to that of the tail tube. The differential roles between gp15 and gp3 upon completion of the tail are discussed.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference27 articles.

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3. Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure

4. Bloomfield, V., W. O. Dalton, and K. E. Van Holde. 1967. Frictional coefficients of multisubunit structures. I. Theory. Biopolymers5:135-148.

5. Coombs D. H. and F. Arisaka. 1994. T4 tail structure and function p. 259-281. In J. D. Karam et al. (ed.) Molecular biology of bacteriophage T4. American Society for Microbiology Washington D.C.

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