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Identification of a novel nuclear speckle-type protein, SPOP

A novel antigen recognized by serum from a scleroderma patient was identified by expression cloning from the HeLa cell cDNA library. The cloned cDNA encoded a 374-amino acid protein with a relative molecular mass of 47 000 and a predicted amino acid sequence 62.7% identical to the hypothetical prote...

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Bibliographic Details
Published in:FEBS letters 1997-11, Vol.418 (1), p.23-26
Main Authors: Nagai, Yasuo, Kojima, Tatsuya, Muro, Yoshinao, Hachiya, Takahisa, Nishizawa, Yuji, Wakabayashi, Takashi, Hagiwara, Masatoshi
Format: Article
Language:English
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Summary:A novel antigen recognized by serum from a scleroderma patient was identified by expression cloning from the HeLa cell cDNA library. The cloned cDNA encoded a 374-amino acid protein with a relative molecular mass of 47 000 and a predicted amino acid sequence 62.7% identical to the hypothetical protein of Caenorhabditis elegans, T16H12.5. The deduced amino acid sequence had a typical POZ domain and an unidentified region conserved during evolution. No zinc finger or RNA recognition motifs were found in this clone. The 2 kbp mRNA encoding the novel clone SPOP (speckle-type POZ protein) was found to be expressed in all human tissues examined. HA-tagged SPOP, transfected and overexpressed in COS7 cells, exhibited a discrete speckled pattern in the nuclei and was co-localized with the splicing factor, snRNP B′/B. Deletion analysis revealed that both the POZ domain and the evolutionarily conserved region at the amino-terminus are required for the nuclear speckled accumulation of SPOP.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)01340-9