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J. Biol. Chem., Vol. 275, Issue 46, 36094-36103, November 17, 2000
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From the Department of Biochemistry, University of Missouri,
Columbia, Missouri 65211
The NMR structure of the N-terminal, DnaJ-like
domain of murine polyomavirus tumor antigens (PyJ) has been determined
to high precision, with root mean square deviations to the mean
structure of 0.38 Å for backbone atoms and 0.94 Å for all heavy atoms
of ordered residues 5-41 and 50-69. PyJ possesses a three-helix fold, in which anti-parallel helices II and III are bridged by helix I,
similar to the four-helix fold of the J domains of DnaJ and human
DnaJ-1. PyJ differs significantly in the lengths of N terminus, helix
I, and helix III. The universally conserved HPD motif appears to form a
His-Pro C-cap of helix II. Helix I features a stabilizing Schellman
C-cap that is probably conserved universally among J domains. On the
helix II surface where positive charges of other J domains have been
implicated in binding of hsp70s, PyJ contains glutamine residues.
Nonetheless, chimeras that replace the J domain of DnaJ with PyJ
function like wild-type DnaJ in promoting growth of Escherichia
coli. This activity can be modulated by mutations of at least one
of these glutamines. T antigen mutations reported to impair cellular
transformation by the virus, presumably via interactions with PP2A,
cluster in the hydrophobic folding core and at the extreme N terminus,
remote from the HPD loop.
The atomic coordinates and the structure factors (code 1faf) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
NMR Structure of the N-terminal J Domain of Murine Polyomavirus T
Antigens
IMPLICATIONS FOR DnaJ-LIKE DOMAINS AND FOR MUTATIONS OF T
ANTIGENS*
*
This work was supported by American Cancer Society Grant
RPG-98-253-1-MBC (to S. R. V.), United States Public Health Service Grant CA38538 (to W. R. F.), and a University of Missouri Research Board grant (to W. R. F.). This is a contribution from the Missouri Agricultural Experiment Station, Journal Series number 13,061.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.
To whom correspondence should be addressed: Dept. of Biochemistry,
117 Schweitzer Hall, University of Missouri, Columbia, MO 65211. Tel.: 573-882-5113; Fax: 573-884-4812; E-mail:
vandorens@missouri.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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