作者: Tomoko Tada , Masayuki Ohmori , Hidetoshi Iida
DOI: 10.1016/J.BBRC.2003.11.166
关键词: Extracellular 、 Saccharomyces cerevisiae 、 Yeast 、 Integral membrane protein 、 Mutation 、 Mutant 、 Amino acid 、 Residue (chemistry) 、 Biology 、 Biochemistry
摘要: The yeast Mid1 protein is an integral membrane required for the viability of differentiated cells and Ca2+ influx induced by mating pheromone. Our previous study has identified a loss-of-function mutation, F356S. F356S mutant completely unable to maintain viability, but still accumulation activity near wild-type level. Here we further examined in detail mutation unravel function Phe356. After exposure pheromone, was not fully rescued high extracellular Ca2+, like mid1 null mutant, suggesting that Phe356 itself are also maintenance mechanism does involve signalling. Substitutions hydrophilic amino acids caused lethality low accumulation, those hydrophobic did not. small significantly reduced affect accumulation. We suggest hydrophobicity residue important both uptake, its size maintenance.