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Journal of Bacteriology, May 1999, p. 2739-2744, Vol. 181, No. 9
Department of Life Science, Faculty of
Bioscience and Biotechnology, Tokyo Institute of Technology,
Nagatuta, Midori-ku, Yokohama 226-8501, Japan,1
and Institute of Molecular Biology and Howard Hughes
Medical Institute, University of Oregon, Eugene, Oregon
97403-12292
Received 2 November 1998/Accepted 17 February 1999
Tail-associated lysozyme of bacteriophage T4 (tail lysozyme), the
product of gene 5 (gp 5), is an essential structural component of the
hub of the phage baseplate. It is synthesized as a 63-kDa precursor,
which later cleaves to form mature gp 5 with a molecular weight of
43,000. To elucidate the role of the C-terminal region of the precursor
protein, gene 5 was cloned and overexpressed and the product was
analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis,
immunoblotting, analytical ultracentrifugation, and circular dichroism.
It was shown that the precursor protein tends to be cleaved into two
fragments during expression and that the cleavage site is close to or
perhaps identical to the cleavage site in the infected cell. The two
fragments, however, remained associated. The lysozyme activity of the
precursor or the nicked protein is about 10% of that of mature gp 5. Both the N-terminal mature tail lysozyme and the C-terminal fragment
were then isolated and characterized by far-UV circular dichroism and
analytical ultracentrifugation. The latter remained trimeric after
dissociation from the N-terminal fragment and is rich in
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The C-Terminal Fragment of the Precursor Tail
Lysozyme of Bacteriophage T4 Stays as a Structural Component of the
Baseplate after Cleavage
-structure
as predicted by an empirical method. To trace the fate of the
C-terminal fragment, antiserum was raised against a synthesized peptide
of the last 12 C-terminal residues. Surprisingly, the C-terminal
fragment was found in the tail and the phage particle by
immunoblotting. The significance of this finding is discussed in
relation to the molecular assembly and infection process.
*
Corresponding author. Mailing address: Department of
Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatuta, Midori-ku, Yokohama 226-8501, Japan. Phone:
81-45-924-5713. Fax: 81-45-924-5805. E-mail:
farisaka{at}bio.titech.ac.jp.
Journal of Bacteriology, May 1999, p. 2739-2744, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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