期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 99, 期 4, 页码 1926-1930出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.042538599
关键词
Saccharomyces cerevisiae; TOK1; channel gating
资金
- NIGMS NIH HHS [R01 GM054867, GM54867] Funding Source: Medline
Non-targeted mutagenesis studies of the yeast K+ channel, TOK1, have led to identification of functional domains common to other cation channels as well as those so far not found in other channels. Among the latter is the ability of the carboxyl tail to prevent channel closure. Here, we show that the tail can fulfill this function in trans. Coexpression of the carboxyl tail with the tail-deleted channel core restores normal channel behavior. A Ser/Thr-rich region at its amino end and an acidic stretch at its carboxyl end delineate the minimal region required for tail function. This region of 160 aa apparently forms a discrete functional domain. Interaction of this domain with the channel core is strong, being recalcitrant to removal from excised membrane patches by both high salt and reducing agents. Although the use of a cytoplasmic domain to regulate channel is common among animal channels, by using it as a foot-in-the-door to maintain open state appears unique to TOM, the first fungal K+ channel studied in depth.
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