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(Received for publication, June 27, 1996, and in revised form, December 11, 1996)
From the NRE1 is a DNA sequence element through which Ku
antigen/DNA-dependent protein kinase (DNA-PK) catalytic
subunit represses the induction of mouse mammary tumor virus
transcription by glucocorticoids. Although Ku is an avid binder of DNA
ends and has the ability to translocate along DNA, we report that
direct sequence-specific Ku binding occurs with higher affinity
(Kd = 0.84 ± 0.24 nM) than DNA
end binding. Comparison of Ku binding to several sequences over which
Ku can accumulate revealed two classes of sequence. Sequences with
similarity to NRE1 competed efficiently for NRE1 binding. Conversely,
sequences lacking similarity to NRE1 competed poorly for Ku and were
not recognized in the absence of DNA ends. Phosphorylation of
glucocorticoid receptor (GR) fusion proteins by DNA-PK reflected Ku
DNA-binding preferences and demonstrated that co-localization of GR
with DNA-PK on DNA in cis was critical for efficient
phosphorylation. Phosphorylation of the GR fusion protein by DNA-PK
mapped to a single site, Ser-527. This site occurs adjacent the GR
nuclear localization sequence between the DNA and ligand binding
domains of GR, and thus its phosphorylation, if confirmed, has the
potential to affect receptor function in vivo.
Volume 272, Number 9,
Issue of February 28, 1997
pp. 5647-5658
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
PHOSPHORYLATION OF Ser-527 OF THE RAT GLUCOCORTICOID
RECEPTOR
,
,
,
,
,§
and§
Departments of Medicine and
§ Biochemistry, University of Ottawa, Loeb Medical Research
Institute, Ottawa Civic Hospital, Ottawa, Ontario, Canada K1Y 4E9 and
the 
Department of Cell Biology, Baylor College of Medicine,
Houston, Texas 77030
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