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

ABSTRACT: 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.

SUBMITTER: Chang YW

PROVIDER: S-EPMC2843242 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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

Chang Yi-Wei YW Chuang Yu-Chien YC Ho Yu-Chi YC Cheng Ming-Yuan MY Sun Yuh-Ju YJ Hsiao Chwan-Deng CD Wang Chung C

The Journal of biological chemistry 20100127 13

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 p ...[more]

PMID: 20106980

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Crystal structure of ATP-bound Get3-Get4-Get5 complex reveals regulation of Get3 by Get4.

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