Crystal structure of Get4-Get5 complex and its interactions with Sgt2, Get3, and Ydj1.

Get3, Get4, and Get5 in Saccharomyces cerevisiae participate in the insertion of tail-anchored proteins into the endoplasmic reticulum membrane. We elucidated the interaction between Get4 and Get5 and investigated their interaction with Get3 and a tetratricopeptide repeat-containing protein, Sgt2. Based on co-immunoprecipitation and crystallographic studies, Get4 and Get5 formed a ...
tight complex, suggesting that they constitute subunits of a larger complex. In contrast, although Get3 interacted physically with the Get4-Get5 complex, low amounts of Get3 co-precipitated with Get5, implying a transient interaction between Get3 and Get4-Get5. Sgt2 also interacted with Get5, although the amount of Sgt2 that co-precipitated with Get5 varied. Moreover, GET3, GET4, and GET5 interacted genetically with molecular chaperone YDJ1, suggesting that chaperones might also be involved in the insertion of tail-anchored proteins.
Mesh Terms:
Adenosine Triphosphatases, Carrier Proteins, Crystallography, X-Ray, Fungal Proteins, Gene Deletion, Gene Expression Profiling, Gene Expression Regulation, Fungal, Guanine Nucleotide Exchange Factors, HSP40 Heat-Shock Proteins, Mass Spectrometry, Molecular Chaperones, Protein Interaction Mapping, Protein Structure, Tertiary, Protein Transport, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques, Ubiquitin
J. Biol. Chem.
Date: Mar. 26, 2010
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