## Abstract The Xβbox binding protein RFX4 is highly expressed in testis in contrast with other tissues, but its function there is unknown. Another family member abundant in testis, RFX2, has been shown to bind to the XβBox elements in the promoter of the testis specific histone H1t, which is expre
Regulation of transcription of the testis-specific histone H1t gene by multiple promoter elements
β Scribed by Sidney R. Grimes; Jane van Wert; Steven A. Wolfe
- Book ID
- 110241515
- Publisher
- Springer
- Year
- 1997
- Tongue
- English
- Weight
- 83 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0301-4851
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Transcription of the mammalian testisβspecific linker histone __H1t__ gene occurs only in pachytene primary spermatocytes during spermatogenesis. Studies of the wild type (Wt) and mutant H1t promoters in transgenic mice show that transcription of the __H1t__ gene is dependent upon the T
The rat testis-specific linker histone H1t gene is transcribed in pachytene primary spermatocytes during spermatogenesis. Our previous work using transgenic mice demonstrated that spermatocyte-specific transcription of the H1t gene is dependent upon a proximal promoter element designated the TE elem
## Abstract The testisβspecific linker histone __H1t__ gene is transcribed exclusively in pachytene primary spermatocytes. Tissue specific expression of the gene is mediated in part by transcriptional factors that bind elements located within the proximal and distal promoter. A 40 bp promoter eleme
The testis-specific histone H1t is synthesized during spermatogenesis exclusively in late pachytene primary spermatocytes. Transcription of the H1t gene is repressed in every tissue except testis. Within the testis, transcription is repressed during development before the spermatocyte stage and in l
Multiple regulatory elements and intricate protein-DNA interactions mediate the transcription of the human histone H4 genes in a cell growth-dependent manner. Upon analysis of the regulatory elements of the FO108 histone H4 gene, we identified several potential YY1 binding sites. In this study, we h