Garcerá Ana, Martínez Ana Isabel, Castillo Luis, Elorza M Victoria, Sentandreu Rafael, Valentín Eulogio
Departamento de Microbiología y Ecología, Facultad de Farmacia, Universidad de Valencia, Avda. Vicente Andrés Estellés s/n, 46100-Burjassot (Valencia), Spain.
Microbiology (Reading). 2003 Aug;149(Pt 8):2137-2145. doi: 10.1099/mic.0.26301-0.
After screening of a Candida albicans genome database, the product of an ORF (IPF 3054) that has 62 % homology with Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein, was identified and named CaSsr1p. The deduced amino acid sequence shows that CaSsr1p contains an N-terminal hydrophobic signal peptide, is rich in Ser and Thr amino acids and has a potential glycosylphosphatidylinositol-attachment signal. CaSsr1p is released following degradation of isolated cell walls by zymolyase (mainly a 1,3-beta-glucanase) and therefore seems to be covalently linked to the beta-glucan of the cell walls. Both disruption and overexpression of the CaSSR1 gene caused an increased sensitivity to calcofluor white, Congo red and zymolyase digestion. These results suggest that CaSsr1p has a structural role associated with the cell-wall beta-glucan.
在筛选白色念珠菌基因组数据库后,鉴定出一个与酿酒酵母Ssr1p(一种细胞内细胞壁蛋白)具有62%同源性的开放阅读框(IPF 3054)的产物,并将其命名为CaSsr1p。推导的氨基酸序列表明,CaSsr1p含有一个N端疏水信号肽,富含丝氨酸和苏氨酸氨基酸,并且具有潜在的糖基磷脂酰肌醇附着信号。在通过溶菌酶(主要是1,3-β-葡聚糖酶)降解分离的细胞壁后,CaSsr1p被释放,因此似乎与细胞壁的β-葡聚糖共价连接。CaSSR1基因的破坏和过表达均导致对荧光增白剂、刚果红和溶菌酶消化的敏感性增加。这些结果表明,CaSsr1p在与细胞壁β-葡聚糖相关的结构中起作用。