| Abstract |
The basic helix-looop-helix (bHLH) family of transcription factors is involved in the regulation of multiple developmental processes, such as neurogenesis, cardiac muscle development, myogenesis and hematopoiesis. bHLH proteins bind to a common DNA sequence (CANNTG) called E-box sequence through the basic domain. Typically they function as homo- or heterodimers. HLH domain is involved in dimerization. bHLH proteins were divided in seven different groups according to their tissue distribution, dimerization capacities or DNA-binding preferences. Class I proteins like ME1, E2 and Da, are ubiquitously expressed and they form homodimers or they heterodimerize with bHLH proteins of class II. Class II proteins, like MASH-1, MATH-1, NeuroD and NSCL-1, have a tissue specific expression pattern. NSCL-1 is expressed mostly in post-mitotic cells, in the developing nervous system. NSCL-1 forms homodimers, but it also heterodimerize with E12 and ME1a. In this study, we investigate the role of NSCL-1 as a transcriptional activator and we try to identify a possible activating domain using the luciferace system. Three versions of the luciferase system have been used. Two of them include a reporter plasmid that has different E-boxes upstream of the luciferase gene. ME1a and truncated forms of NSCL-1 have been used in order to activate the luciferase gene. The third system includes a reporter plasmid that has the UAS region upstream of the luciferase gene. Truncated forms of NSCL-1 fused to the GAL4 domain were tested in order to identify a possible activating domain of NSCL-1. 5
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Συμβολή στη μελέτη της δράσης του μεταγραφικού παράγοντα NSCL-1
