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J. Biol. Chem., Vol. 276, Issue 1, 449-456, January 5, 2001
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From the Division of Infection, Immunity, Injury, and Repair,
Research Institute, Hospital for Sick Children, Toronto,
Ontario M5G 1X8, Canada, the The region(s) of hsp70 critical for
sulfogalactolipid (SGL) recognition has been defined through deletion
analysis and site-directed mutagenesis. Truncated polymerase
chain reaction products of hsp70 generated N-terminal fragments of 43, 35, 29, and 22 kDa. The C terminus substrate-binding domain (28 kDa)
was also expressed. The N-terminal ATPase domain (rP43) shared the
binding specificity of hsp70, because only sulfogalactosyl ceramide and
sulfogalactosyl glycerolipid were recognized by both TLC overlay and
RELISA. The C-terminal domain showed no binding. SGL binding of rP29
and rP22 was severely reduced. The loss of SGL binding for rP35 by
RELISA but not TLC overlay was considered as a function of receptor
presentation. The truncation of rP43 to rP35 demonstrates that
residues 318-387 (the base of the ATP binding cleft) are critical for
high affinity SGL binding. Mutagenesis showed that
Arg342 and Phe198 are crucial for
this process. SGL binding, mediated by these conserved residues within
the ATPase domain of hsp70, implies that this binding specificity is
evolutionarily conserved.
The ATPase Domain of hsp70 Possesses a Unique Binding Specificity
for 3'-Sulfogalactolipids*
and§¶
Department of Laboratory
Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5G
1L5, Canada, and the § Department of Biochemistry,
University of Toronto, Toronto, Ontario M5S 1A8, Canada
*
This study was supported by Medical Research Council
Grant MT 14367 and a Medical Research Council Studentship (to D. M.).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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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