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Publication : Structure and functional characterization of single-strand DNA binding protein SSDP1: carboxyl-terminal of SSDP1 has transcription activity.

First Author  Wu L Year  2006
Journal  Biochem Biophys Res Commun Volume  339
Issue  3 Pages  977-84
PubMed ID  16325762 Mgi Jnum  J:104885
Mgi Id  MGI:3613092 Doi  10.1016/j.bbrc.2005.11.098
Citation  Wu L (2006) Structure and functional characterization of single-strand DNA binding protein SSDP1: carboxyl-terminal of SSDP1 has transcription activity. Biochem Biophys Res Commun 339(3):977-84
abstractText  LIM-homeodomain transcription factors control a wide range of developmental processes, such as early patterning of the embryonic development, organ formations of brain, limbs, and eyes. Molecular mechanisms of the underlying processes involve complicated multiple protein complexes that direct transcription activation of target genes, protein-protein interactions, and transcriptional regulations. Among those molecules, cofactor Ldb1, interacting with LIM/homeobox family transcription factor, defines a tetrameric protein complex in controlling downstream genes of transcriptional regulation. In addition, SSDP specifically involves this complex supported by showing that both SSDP1 and SSDP2 bind to Ldb1 in vivo. Here it has been found that SSDP1 itself is a transcription factor that has transcription activity independently. Furthermore, C-terminal of SSDP1 possessing an entire transcription activity in vivo, confirmed in both yeast and mammalian cells, has been defined. Interestingly, the transcriptional function of SSDP1 was not required for the interaction with Ldb1. Thus, biochemical data of SSDP1 presented by this study provides biochemical evidence for a better understanding of transcriptional regulation.
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