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Crystal structure of Ski8p, a WD‐repeat protein with dual roles in mRNA metabolism and meiotic recombination
Author(s) -
Cheng Zhihong,
Liu Yuying,
Wang Chernhoe,
Parker Roy,
Song Haiwei
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.04856504
Subject(s) - homologous recombination , saccharomyces cerevisiae , messenger rna , meiosis , biology , recombination , mutagenesis , genetics , protein structure , amino acid , microbiology and biotechnology , yeast , gene , biochemistry , mutation
Abstract Ski8p is a WD‐repeat protein with an essential role for the Ski complex assembly in an exosome‐dependent 3′‐to‐5′ mRNA decay. In addition, Ski8p is involved in meiotic recombination by interacting with Spo11p protein. We have determined the crystal structure of Ski8p from Saccharomyces cerevisiae at 2.2 Å resolution. The structure reveals that Ski8p folds into a seven‐bladed β propeller. Mapping sequence conservation and hydrophobicities of amino acids on the molecular surface of Ski8p reveals a prominent site on the top surface of the β propeller, which is most likely involved in mediating interactions of Ski8p with Ski3p and Spo11p. Mutagenesis combined with yeast two‐hybrid and GST pull‐down assays identified the top surface of the β propeller as being required for Ski8p binding to Ski3p and Spo11p. The functional implications for Ski8p function in both mRNA decay and meiotic recombination are discussed.