Transcriptional activation modulated by homopolymeric glutamine and proline stretches.
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.
Gerber
H P
HP
Institut für Molekularbiologie II der Universität Zürich, Switzerland.
Seipel
K
K
Georgiev
O
O
Höfferer
M
M
Hug
M
M
Rusconi
S
S
Schaffner
W
W
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D005973:Glutamine / Q000737:chemistry* / Q000494:pharmacology; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology; D011993:Recombinant Fusion Proteins / Q000494:pharmacology; D012091:Repetitive Sequences, Nucleic Acid; D014157:Transcription Factors / Q000737:chemistry* / Q000494:pharmacology; D015533:Transcriptional Activation; D014162:Transfection
D010455:Peptides; D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; D005973:Glutamine; C011083:polyproline