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J. Biol. Chem., Vol. 276, Issue 19, 15571-15574, May 11, 2001
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From the Departments of The ribonucleoprotein telomerase
holoenzyme is minimally composed of a catalytic subunit, hTERT, and its
associated template RNA component, hTR. We have previously found two
additional components of the telomerase holoenzyme, the chaperones p23
and heat shock protein (hsp) 90, both of which are required for
efficient telomerase assembly in vitro and in
vivo. Both hsp90 and p23 bind specifically to hTERT and influence
its proper assembly with the template RNA, hTR. We report here that the
hsp70 chaperone also associates with hTERT in the absence of hTR and
dissociates when telomerase is folded into its active state, similar to
what occurs with other chaperone targets. Our data also indicate that
hsp90 and p23 remain associated with functional telomerase complexes,
which differs from other hsp90-folded enzymes that require only a
transient hsp90·p23 binding. Our data suggest that components of the
hsp90 chaperone complex, while required for telomerase assembly, remain associated with active enzyme, which may ultimately provide critical insight into the biochemical properties of telomerase assembly.
ACCELERATED PUBLICATION
Stable Association of hsp90 and p23, but Not hsp70, with Active
Human Telomerase*
,,,, and§¶
Pathology and
§ Human Genetics, Massey Cancer Center, Medical College of
Virginia at Virginia Commonwealth University, Richmond, Virginia
23298-0662
*
This work was supported by the V foundation (to S. E. H.),
the Mary Kay Ash Foundation (to S. E. H.), and the Howard Hughes Medical Institute (to J. L. J.).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.
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