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J. Biol. Chem., Vol. 276, Issue 27, 25386-25391, July 6, 2001
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From the In a previous study, we demonstrated that the
forkhead associated (FHA) domain of pKi-67 interacts with the novel
kinesin-like protein, Hklp2 (Sueishi, M., Takagi, M., and Yoneda, Y. (2000) J. Biol. Chem. 275, 28888-28892). In this
study, we report on the identification of a putative RNA-binding
protein of 293 residues as another binding partner of the FHA domain of
pKi-67 (referred to as NIFK for nucleolar protein
interacting with the FHA domain of
pKi-67). Human NIFK (hNIFK) interacted with the FHA domain of pKi-67 (Ki-FHA) efficiently in vitro when hNIFK was
derived from mitotically arrested cells. In addition, a moiety of hNIFK was co-localized with pKi-67 at the peripheral region of mitotic chromosomes. The hNIFK domain that interacts with Ki-FHA was mapped in
the yeast two-hybrid system to a portion encompassed by residues 226-269. In a binding assay utilizing Xenopus egg
extracts, it was found that the mitosis-specific environment and two
threonine residues within this portion of hNIFK (Thr-234 and Thr-238)
were crucial for the efficient interaction of hNIFK and Ki-FHA,
suggesting that hNIFK interacts with Ki-FHA in a mitosis-specific and
phosphorylation-dependent manner. These findings provide a
new clue to our understanding of the cellular function of
pKi-67.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB044971 and AB056870.
A Novel Nucleolar Protein, NIFK, Interacts with the
Forkhead Associated Domain of Ki-67 Antigen in Mitosis*
,,,, and§¶
Department of Cell Biology and Neuroscience,
Graduate School of Medicine, Osaka University, 2-2 Yamada-oka, Suita,
Osaka 565-0871 and the § Institute for Molecular and
Cellular Biology, Osaka University, 1-3 Yamada-oka, Suita,
Osaka 565-0871, Japan
*
This work was supported by Grant-in-aid for Scientific
Research on Priority Areas (B) 11237202, Grant-in-aid for Scientific Research (B) 12480215, Grant-in-aid for COE Research 12CE2007 from the
Japanese Ministry of Education, Science, Sports and Culture, the
Mitsubishi Foundation, and the Human Frontier Science Program.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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