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J. Biol. Chem., Vol. 276, Issue 44, 41064-41072, November 2, 2001
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From the Department of Physiology, the University of Texas
Southwestern Medical Center, Dallas, Texas 75390-9040
Phosphorylation of circadian clock proteins
represents a major regulatory step that controls circadian clocks. In
Neurospora, the circadian clock protein FREQUENCY (FRQ) is
progressively phosphorylated over time, and its level decreases when it
is hyperphosphorylated. In this study, we showed that most of the
kinase activity phosphorylating FRQ in vitro was
calcium/calmodulin-dependent, and the endogenous FRQ in the
Neurospora extracts was phosphorylated by a
Ca/CaM-dependent kinase-like activity. From
Neurospora cell extracts, an ~50-kDa Ca/CaM-dependent kinase (CAMK-1) that can specifically
phosphorylate FRQ was purified. In vitro, this kinase
accounts for near half of the FRQ kinase activity, and it can
phosphorylate the FRQ region that contains the three known
functionally important phosphorylation sites. To understand the
function of camk-1 in vivo, it was disrupted in
Neurospora by gene replacement. After germination from
ascospores, the camk-1 null strains grew slowly, indicating
that CAMK-1 plays an important role in growth and development of
Neurospora. This phenotype was transient however, revealing
redundancy in the system. Analysis of the camk-1 null
strain revealed that the deletion of camk-1 affected phase,
period, and light-induced phase shifting of the circadian
conidiation rhythm. Taken together, our results suggest that
multiple kinases may phosphorylate FRQ in vivo.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AY052653.
Identification of a Calcium/Calmodulin-dependent
Protein Kinase That Phosphorylates the Neurospora Circadian
Clock Protein FREQUENCY*
*
This work was supported by Grant GM 62591 from the National
Institutes of Health (to Y. L.).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.
Louise W. Kahn Scholar in Biomedical Research at the University of
Texas Southwestern Medical Center. To whom correspondence should be
addressed: Dept. of Physiology, the University of Texas Southwestern
Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9040. Tel.: 214-648-3701; Fax: 214-648-7891; E-mail:
Yi.Liu@UTsouthwestern.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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