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

Institute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.
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. Mar. 26, 2010; 285(13);9962-70 [PUBMED:20106980]
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