Open AccessFar3p domains involved in the interactions of Far proteins and pheromone‐induced cell cycle arrest in budding yeast
Author(s) -
Lai Fenju,
Wu Rentian,
Wang Jiafeng,
Li Chunming,
Zou Lan,
Lu Yongjun,
Liang Chun
Publication year - 2011
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2010.00691.x
Subject(s) - coiled coil , biology , budding yeast , microbiology and biotechnology , mutant , cell cycle protein , cell cycle , mutation , function (biology) , saccharomyces cerevisiae , genetics , yeast , cell , gene
Far3p (factor arrest), a protein that interacts with Far7–11p, is required for the pheromone‐mediated cell cycle arrest in G1 phase. We used a combination of computational and experimental strategies to identify the Far3p self‐association, to map the Far3p domains that interact with Far3p itself and with other Far proteins, and to reveal the importance of the two coiled‐coil motifs of Far3p in the integrity and function of the Far complex. We show that Far3p self‐associates through its central region and its C‐terminal coiled‐coil domain, that the amino acid 61–100 region of Far3p interacts with Far7p, and that the Far3p N‐terminal coiled‐coil domain interacts with Far9p and Far10p. Mutation of the N‐terminal coiled coil disrupts the interactions of Far3p with Far9p and Far10p, and mutation of the C‐terminal domain weakens the Far3p self‐interaction. Although the N‐ and C‐terminal coiled‐coil mutants reserve some of the interactions with itself and some other Far proteins, both mutants are defective in the pheromone‐mediated G1 arrest, indicating that both coiled‐coil motifs of Far3p are essential for the integrity and the function of the Far complex.