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J. Biol. Chem., Vol. 278, Issue 15, 12634-12644, April 11, 2003
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From the Bacteriophages infecting the
neuroinvasive pathogen Escherichia coli K1 require an
endosialidase to penetrate the polysialic acid capsule of the host.
Sequence information is available for the endosialidases endoNE,
endoNF, and endoN63D of the K1-specific phages The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AJ505988.
Proteolytic Processing and Oligomerization of
Bacteriophage-derived Endosialidases*
§,,,
, and
Abteilung Zelluläre Chemie, Zentrum
Biochemie, Medizinische Hochschule Hannover, Carl-Neuberg-Strasse
1, 30625 Hannover and the ¶ Institut für Mikro-
und Molekularbiologie, Justus-Liebig-Universität Giessen,
Ludwigstrasse 23, D-35390 Giessen, Germany
K1E, K1F,
and 63D, respectively. The cloned sequences share a highly conserved
catalytic domain but differ in the length of the N- and C-terminal
parts. Although the expression of active recombinant enzyme succeeded
in the case of endoNE, it failed for endoNF. Protein alignments of all
three endosialidase sequences gave rise to the assumption that
inactivity of the cloned endoNF is caused by a C-terminal truncation.
By reinvestigation of the respective gene locus in the K1F genome,
we identified an extended open reading frame of 3195 bp, encoding a
119-kDa protein. Full-length endoNF contains the C-terminal domain
conserved in all endosialidases, which may act as an intramolecular
chaperone. Comparative studies carried out with endoNE and endoNF
demonstrate that endosialidases are proteolytically processed,
releasing the C-terminal domain. Using a mutational approach in
combination with protein analytical techniques we demonstrate that (i)
the C-terminal domain is a common feature of endosialidases and other
tail fiber proteins; (ii) the integrity of the C-terminal domain and
its presence in the nascent protein are crucial for the formation of
active enzymes; (iii) proteolytic processing is not essential for
enzymatic activity; and (iv) functional folding is a prerequisite for
trimerization of endoNF.
*
This work was supported by Deutsche Forschungsgemeinschaft
Grant GE 801/3-3 and by the Fonds der Chemischen Industrie.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: BESSY GmbH, Albert-Einstein-Strasse 15, Berlin 12469, Germany.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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