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© The Rockefeller University Press, 0021-9525/1997//899 $5.00
The Journal of Cell Biology, Volume 137, Number 4, , 1997 899-908

Article

A Glycine-rich RNA-binding Protein Mediating Cold-inducible Suppression of Mammalian Cell Growth



Hiroyuki Nishiyama*,{ddagger}, Katsuhiko Itoh*, Yoshiyuki Kaneko*, Masamichi Kishishita*, Osamu Yoshida{ddagger}, and Jun Fujita*

* Department of Clinical Molecular Biology, {ddagger} Department of Urology, Faculty of Medicine, Kyoto University, Kyoto 606, Japan

In response to low ambient temperature, mammalian cells as well as microorganisms change various physiological functions, but the molecular mechanisms underlying these adaptations are just beginning to be understood. We report here the isolation of a mouse cold-inducible RNA-binding protein (cirp) cDNA and investigation of its role in cold-stress response of mammalian cells. The cirp cDNA encoded an 18-kD protein consisting of an amino-terminal RNAbinding domain and a carboxyl-terminal glycine-rich domain and exhibited structural similarity to a class of stress-induced RNA-binding proteins found in plants. Immunofluorescence microscopy showed that CIRP was localized in the nucleoplasm of BALB/3T3 mouse fibroblasts. When the culture temperature was lowered from 37 to 32°C, expression of CIRP was induced and growth of BALB/3T3 cells was impaired as compared with that at 37°C. By suppressing the induction of CIRP with antisense oligodeoxynucleotides, this impairment was alleviated, while overexpression of CIRP resulted in impaired growth at 37°C with prolongation of G1 phase of the cell cycle. These results indicate that CIRP plays an essential role in cold-induced growth suppression of mouse fibroblasts. Identification of CIRP may provide a clue to the regulatory mechanisms of cold responses in mammalian cells.

Abbreviations used in this paper: CIRP, cold-inducible RNA-binding protein; CS-RBD, consensus sequence RNA-binding domain; GFP, green fluorescence protein; GRP, glycine-rich RNA-binding protein; GST, glutathione-S-transferase; ODN, oligodeoxynucleotide; RNP, ribonucleoprotein.

This work was partly supported by Grants-in-Aid from the Ministry of Education, Science, Sports, and Culture of Japan.

Address all correspondence to Jun Fujita, Department of Clinical Molecular Biology, Faculty of Medicine, Kyoto University, Shogoin Kawaharacho, Sakyo-ku, Kyoto 606, Japan. Tel.: 81-75-751-3751. Fax: 81-75-7513750. E-mail: jfujita{at}virus.kyoto-u.ac.jp


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