Transcriptional Activation Modulated by Homopolymeric Glutamine and Proline Stretches

• Published in: Science (American Association for the Advancement of Science) 1994-02, Vol.263 (5148), p.808-811
• Main Authors: Gerber, Hans-Peter, Seipel, Katja, Georgiev, Oleg, Höfferer, Manuela, Hug, Martin, Rusconi, Sandro, Schaffner, Walter
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Animals; Base Sequence; Biological and medical sciences; Cell Line; COS cells; DNA; Drosophila; Fundamental and applied biological sciences. Psychology; Genetic diseases; Glutamine - chemistry; Glutamine - pharmacology; HeLa Cells; Humans; Huntington disease; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Myotonic dystrophy; Peptides - chemistry; Peptides - pharmacology; Recombinant Fusion Proteins - pharmacology; Repetitive Sequences, Nucleic Acid; Transcription factors; Transcription Factors - chemistry; Transcription Factors - pharmacology; Transcription. Transcription factor. Splicing. Rna processing; Transcriptional Activation; Transfection
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.8303297

Many transcription factors contain proline- or glutamine-rich activation domains. Here it is shown that simple homopolymeric stretches of these amino acids can activate transcription when fused to the DNA binding domain of GAL4 factor. In vitro, activity increased with polymer length, whereas in cell transfection assays maximal activity was achieved by 10 to 30 glutamines or about 10 prolines. Similar results were obtained when glutamine stretches were placed within a [GAL4]-VP16 chimeric protein. Because these stretches are encoded by rapidly evolving triplet repeats (microsatellites), they may be the main cause for modulation of transcription factor activity and thus result in subtle or overt genomic effects.