Identification and analysis of the promoter region of the type II transmembrane serine protease polyserase-1 and its transcript variants
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Masaki Hayama
Abstract
Polyserase-1/TMPRSS9 and its alternative transcripts, serase-1B and serase-2B, are novel type II transmembrane serine proteases that may regulate physiological and pathological phenomena on the cell surface. To understand the mechanisms of gene expression and regulation of these transcripts, we cloned and characterized the 5′ promoter region of the mouse polyserase-1 (mpolyserase-1) gene. Using 5′-rapid amplification of cDNA ends, we located the transcription initiation site 272 nucleotides upstream of the translation initiation site. Luciferase reporter gene analysis revealed that the region from +186 to +272 bp in the 5′-untranslated region (UTR), containing the GATA motif (AGATAA), glucocorticoid responsible element (TGTTCT), and E-box sequence (CAGGTG), is required for maximal promoter activity. Mutations introduced into the E-box sequence but not elsewhere in the promoter region caused a selective decrease in transcriptional activity. Furthermore, a DNA probe (+229 to +255 bp) containing the E-box sequence formed a single nuclear protein complex in a sequence-specific manner. These data suggest that the expression of mpolyserase-1 and its transcript variants is positively regulated by the E-box in its 5′-UTR, which might be responsible for the binding of basic helix-loop-helix transcription factors involved in the development of various organelles.
©2007 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Protein import into chloroplasts: new aspects of a well-known topic
- Effect of bleomycin and cisplatin on the expression profile of SRA1, a novel member of pre-mRNA splicing factors, in HL-60 human promyelocytic leukemia cells
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- Alkaline Bohr effect of bird hemoglobins: the case of the flamingo
- Chemical chaperone-mediated protein folding: stabilization of P22 tailspike folding intermediates by glycerol
- The central domain of transcription factor FOXM1c directly interacts with itself in vivo and switches from an essential to an inhibitory domain depending on the FOXM1c binding site
- The structure of CMS2MS2, a mitogenic protein isolated from Carica candamarcensis
- The proteome of the heterocyst cell wall in Anabaena sp. PCC 7120
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