Wiederrecht G, Seto D, Parker C S
Division of Chemistry, California Institute of Technology, Pasadena 91125.
Cell. 1988 Sep 9;54(6):841-53. doi: 10.1016/s0092-8674(88)91197-x.
The yeast heat shock transcription factor gene, HSF1, has been isolated from an S. cerevisiae genomic expression library (in lambda gt11). The sequenced gene encodes an 833 amino acid protein having a mass of 93,218 daltons. Expression of specific DNA-binding activity in E. coli and of transcriptional activity in yeast confirmed the identity of the cloned gene. Southern analysis and gene-disruption experiments indicate that the heat shock transcription factor is encoded by a single-copy, essential gene. The DNA-binding domain was localized to a 118 amino acid region in the amino-terminal third of the protein. Inspection of the DNA-binding domain reveals no resemblance to any currently known secondary structural motifs implicated in DNA recognition and binding.
酵母热休克转录因子基因HSF1已从酿酒酵母基因组表达文库(λgt11载体)中分离出来。测序后的该基因编码一个含833个氨基酸的蛋白质,分子量为93,218道尔顿。在大肠杆菌中表达的特异性DNA结合活性以及在酵母中表达的转录活性证实了克隆基因的身份。Southern分析和基因敲除实验表明,热休克转录因子由一个单拷贝的必需基因编码。DNA结合结构域定位于该蛋白质氨基端三分之一区域内一个含118个氨基酸的区域。对该DNA结合结构域的检查发现,它与目前已知的任何参与DNA识别和结合的二级结构基序均无相似之处。