Ashby M N, Errada P R, Boyartchuk V L, Rine J
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Yeast. 1993 Aug;9(8):907-13. doi: 10.1002/yea.320090810.
We isolated a mutant defective in C-terminal farnesyl cysteine:carboxyl methyltransferase activity from a screen for mutations causing a-specific sterility. A genomic fragment was cloned from a yeast multi-copy library that restored mating. Both the cloned gene and the sterile mutation were allelic to the STE14 gene. A ste14-complementing 2.17 kb BamHI fragment subclone was sequenced and found to encode a 239 amino acid protein with a molecular weight of 27,887 Daltons. The hydrophobicity profile of the methyltransferase reveals the presence of at least five potential transmembrane domains. In comparisons of the C-terminal methyltransferase amino acid sequence with those in the PIR and Swiss protein databases, no significantly similar sequences were found nor were conserved regions from other methyltransferases present.
我们从一个导致α特异性不育的突变筛选中分离出一个在C端法尼基半胱氨酸羧基甲基转移酶活性方面有缺陷的突变体。从酵母多拷贝文库中克隆了一个能恢复交配的基因组片段。克隆的基因和不育突变都与STE14基因等位。对一个能互补ste14的2.17 kb BamHI片段亚克隆进行了测序，发现它编码一个分子量为27,887道尔顿的239个氨基酸的蛋白质。甲基转移酶的疏水性图谱显示至少存在五个潜在的跨膜结构域。将C端甲基转移酶的氨基酸序列与PIR和瑞士蛋白质数据库中的序列进行比较，未发现明显相似的序列，也未发现其他甲基转移酶的保守区域。
