Structural characterization of the Get4/Get5 complex and its interaction with Get3
The recently elucidated Get proteins are responsible for the targeted delivery of the majority of tail-anchored (TA) proteins to the endoplasmic reticulum. Get4 and Get5 have been identified in the early steps of the pathway mediating TA substrate delivery to the cytoplasmic targeting factor Get3. H...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2010-07, Vol.107 (27), p.12127-12132 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Chartron, Justin W. Suloway, Christian J. M. Zaslaver, Ma'ayan Clemons, William M. Rees, Douglas C. |
| description | The recently elucidated Get proteins are responsible for the targeted delivery of the majority of tail-anchored (TA) proteins to the endoplasmic reticulum. Get4 and Get5 have been identified in the early steps of the pathway mediating TA substrate delivery to the cytoplasmic targeting factor Get3. Here we report a crystal structure of Get4 and an N-terminal fragment of Get5 from Saccharomyces cerevisae. We show Get4 and Get5 (Get4/5) form an intimate complex that exists as a dimer (two copies of Get4/5) mediated by the C-terminus of Get5. We further demonstrate that Get3 specifically binds to a conserved surface on Get4 in a nucleotide dependent manner. This work provides further evidence for a model in which Get4/5 operates upstream of Get3 and mediates the specific delivery of a TA substrate. |
| doi_str_mv | 10.1073/pnas.1006036107 |
| format | Article |
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M. ; Zaslaver, Ma'ayan ; Clemons, William M. ; Rees, Douglas C.</creator><creatorcontrib>Chartron, Justin W. ; Suloway, Christian J. M. ; Zaslaver, Ma'ayan ; Clemons, William M. ; Rees, Douglas C.</creatorcontrib><description>The recently elucidated Get proteins are responsible for the targeted delivery of the majority of tail-anchored (TA) proteins to the endoplasmic reticulum. Get4 and Get5 have been identified in the early steps of the pathway mediating TA substrate delivery to the cytoplasmic targeting factor Get3. Here we report a crystal structure of Get4 and an N-terminal fragment of Get5 from Saccharomyces cerevisae. We show Get4 and Get5 (Get4/5) form an intimate complex that exists as a dimer (two copies of Get4/5) mediated by the C-terminus of Get5. We further demonstrate that Get3 specifically binds to a conserved surface on Get4 in a nucleotide dependent manner. 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M.</creatorcontrib><creatorcontrib>Zaslaver, Ma'ayan</creatorcontrib><creatorcontrib>Clemons, William M.</creatorcontrib><creatorcontrib>Rees, Douglas C.</creatorcontrib><title>Structural characterization of the Get4/Get5 complex and its interaction with Get3</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The recently elucidated Get proteins are responsible for the targeted delivery of the majority of tail-anchored (TA) proteins to the endoplasmic reticulum. Get4 and Get5 have been identified in the early steps of the pathway mediating TA substrate delivery to the cytoplasmic targeting factor Get3. Here we report a crystal structure of Get4 and an N-terminal fragment of Get5 from Saccharomyces cerevisae. We show Get4 and Get5 (Get4/5) form an intimate complex that exists as a dimer (two copies of Get4/5) mediated by the C-terminus of Get5. We further demonstrate that Get3 specifically binds to a conserved surface on Get4 in a nucleotide dependent manner. 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| subjects | Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Binding Sites Biochemistry Biological Sciences Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Crystal structure Crystallography, X-Ray Cytoplasm Dimerization Dimers Escherichia coli - genetics Genetic Complementation Test Guanine Nucleotide Exchange Factors - chemistry Guanine Nucleotide Exchange Factors - genetics Guanine Nucleotide Exchange Factors - metabolism Membrane Proteins Models, Molecular Monomers Mutation Nucleotides Phenotypes Protein Binding Protein Interaction Mapping Protein Structure, Tertiary Proteins Recombinant Proteins - chemistry Recombinant Proteins - metabolism Ribosomes Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Substrate Specificity Ubiquitin - chemistry Ubiquitin - genetics Ubiquitin - metabolism Yeast Yeasts |
| title | Structural characterization of the Get4/Get5 complex and its interaction with Get3 |
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