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Department of Chemistry and Bioengineering,3 Graduate School of Engineering,
Department of Environment and Natural Sciences,4 Graduate School of Environment and Information Sciences, Yokohama National University, Yokohama 240-0851, Japan
Department of Genetic Information,5 School of Medicine, Tokai University, Isehara 259-1153, Japan
Paraspeckle protein 1 (PSP1) in humans is a recently identified component protein of a novel nuclear body, paraspeckle. The protein has a DBHS (Drosophila behavior, human splicing) motif that is found in PSF and p54nrb/NonO proteins. These DBHS-containing proteins have been reported to be involved in various nuclear events such as DNA replication, transcription, and mRNA processing. Here we show that mouse paraspeckle protein 1 (mPSP1; encoded by the Pspc1 gene) has two isoforms with different C-termini lengths. Abundant expression of the longer isoform (mPSP1-
) and the shorter one (mPSP1-ß) were observed in testis and kidney, respectively. Transiently expressed mPSP1-
was localized in nuclei, but mPSP1-ß was localized in both nuclei and cytoplasm. These observations suggest that alternative splicing regulates tissue distribution and subcellular localization. Like other DBHS-containing proteins, mPSP1 has RNA-binding activity. In mouse testis, mPSP1-
was found in the nuclear matrix fraction. Furthermore, by coimmunoprecipitation, we confirmed that mPSP1 interacts with other DBHS-containing proteins, PSF and p54nrb/NonO. Therefore, we conclude that mPSP1 may regulate multiple phases of important nuclear events during spermatogenesis.
2 Correspondence: Yasuyuki Kurihara, Department of Environment and Natural Sciences, Graduate School of Environment and Information Sciences, Yokohama National University, Tokiwa-dai, Hodogaya, Yokohama 240-8501, Japan. FAX: 81 45 339 4263; kurihara{at}mac.bio.bsk.ynu.ac.jp
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