Functional study of Saccharomyces cerevisiae alpha factor C- terminal peptide in secretion pathway

• Main Authors: Shu, Lung-Chung, 許綸中
• Other Authors: Tsong-Teh,Kuo
• Format: Others
• Language: zh-TW
• Published: 1997
• Online Access: http://ndltd.ncl.edu.tw/handle/64536474487793852029

碩士 === 中國文化大學 === 生物科技研究所 === 85 === There are two mating types of the haploid Saccharomyces cerevisiae alpha and a . An alpha haploid cell type secretes the alpha mating factor and an a cell type secretes the a factor . The alphais a short pheromonepeptie which contains 13 amino acids . The first 6 amino-acid residues in the N-terminal sequenceof the alpha factor are responsible for the divisionarrest of the a-type S.cerevisiae . However the function of the other 7 C-terminal amino acids of the alpha factor( alpha7) is still unknow . Although the secretion pathway of the alpha factor has been described by alot of previous studies . little information is available on the sorting of the alpha factor in trans golgi . To obtain more information on the function of the alpha7 , we synthesized the nucleotides coding for the alpha7 and ligated this gene cassette to a reporter gene , the green fluorescent protein (GFP) . By detecting the green fluorescence , the distribution of the GFPalpha7fusion protein is monitored . On the basis of this stratagem , we were ableto examine the hypothesis that the alpha7 play an important role in sortingof the alpha factor from trans golgi to vesicles and , thus , to secrete outside the cell . A signal peptide in N-terminal of GFP was found to be required for the introduction of the GFPalpha7 fusion protein into secretion pathway .