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[Structural and functional analysis of the human ribosomal protein L11 gene]
E N Voronina1, T D Kolokol'tsova, E A Nechaeva
1Novosibirsk Institute of Bioorganic Chemistry, Siberian Division, Russian Academy of Sciences, Novosibirsk, 630090 Russia. voronina_l@yahoo.com
Abstract:
The nucleotide sequence was established for the human ribosomal protein L11 gene (HRPL11). The gene (4583 bp) proved to consist of six exons and five introns. The structure of the HRPL11 promoter was shown to be typical for ribosomal protein genes of higher eukaryotes: the promoter lacks TATA or CAAT boxes and has a TATA-like element (ATAA, -24 ... -27) surrounded by GC-rich regions, the transcription start point is within an oligopyrimidine tract, and the 5'-untranslater region is short (26 bp). Proteins interacting with the HRPL11 promoter were identified by the electrophoretic mobility shift assay with oligonucleotide competitors containing known transcription factor-binding sites. The promoter regions were compared for the human genes for ribosomal proteins L11, L32, and S26.