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Molecular and Cellular Biology, March 2005, p. 1779-1792, Vol. 25, No. 5
0270-7306/05/$08.00+0 doi:10.1128/MCB.25.5.1779-1792.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
An Acidic Protein, YBAP1, Mediates the Release of YB-1 from mRNA and Relieves the Translational Repression Activity of YB-1
Ken Matsumoto,*
Kimio J. Tanaka, and
Masafumi Tsujimoto
Laboratory of Cellular Biochemistry, RIKEN, Wako, Saitama, Japan
Received 27 August 2004/
Returned for modification 11 October 2004/
Accepted 30 November 2004
Eukaryotic Y-box proteins are nucleic acid-binding proteins implicated in a wide range of gene regulatory mechanisms. They contain the cold shock domain, which is a nucleic acid-binding structure also found in bacterial cold shock proteins. The Y-box protein YB-1 is known to be a core component of messenger ribonucleoprotein particles (mRNPs) in the cytoplasm. Here we disrupted the YB-1 gene in chicken DT40 cells. Through the immunoprecipitation of an epitope-tagged YB-1 protein, which complemented the slow-growth phenotype of YB-1-depleted cells, we isolated YB-1-associated complexes that likely represented general mRNPs in somatic cells. RNase treatment prior to immunoprecipitation led to the identification of a Y-box protein-associated acidic protein (YBAP1). The specific association of YB-1 with YBAP1 resulted in the release of YB-1 from reconstituted YB-1-mRNA complexes, thereby reducing the translational repression caused by YB-1 in the in vitro system. Our data suggest that YBAP1 induces the remodeling of YB-1-mRNA complexes.
* Corresponding author. Mailing address: Laboratory of Cellular Biochemistry, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Phone: 81-48-467-9764. Fax: 81-48-462-4670. E-mail:
matsumok{at}postman.riken.go.jp.
K.M. dedicates this work to the memory of Alan P. Wolffe.
Molecular and Cellular Biology, March 2005, p. 1779-1792, Vol. 25, No. 5
0022-538X/05/$08.00+0 doi:10.1128/MCB.25.5.1779-1792.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
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