The Amino-terminal domain of tntegrin beta3 functions as a transcriptional activator in yeast.
A deletion mutant encoding the integrin beta3(4I-F56) with an additional Gln at the carboxyl terminus was found occassionally when we were constructing a counterselection yeast two-hybrid assay modle. This mutant exhibited strong transcriptional activation in yeast cells, bearing the Escherichia coli lacZ reporter gene encoding the beta-galactosidase under the transcriptional control of GAL4 promoter and TATA box. Further analysis revealed that the region between the amino acid residues 23C to S77, an acidic domain involved in the function of several transcriptional activators were critical for optimal level of transactivation.
Yang
Jianbo
J
State Key Laboratory of Pharmaceutical Biotechnology, College of Life Science, Nanjing University, Nanjing, 210093, China. yangjie@nju.edu.cn
Yao
Jia
J
Chen
Lili
L
Yang
Jie
J
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D017930:Genes, Reporter; D039661:Integrin beta3 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D010957:Plasmids; D017434:Protein Structure, Tertiary / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D017384:Sequence Deletion; D012694:Serine / Q000235:genetics / Q000378:metabolism; D016385:TATA Box; D015534:Trans-Activators / Q000737:chemistry*; D015533:Transcriptional Activation; D020798:Two-Hybrid System Techniques
D039661:Integrin beta3; D015534:Trans-Activators; D012694:Serine