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Get5 carboxyl-terminal domain is a novel dimerization motif that tethers an extended Get4/Get5 complex.

ABSTRACT: Tail-anchored trans-membrane proteins are targeted to membranes post-translationally. The proteins Get4 and Get5 form an obligate complex that catalyzes the transfer of tail-anchored proteins destined to the endoplasmic reticulum from Sgt2 to the cytosolic targeting factor Get3. Get5 forms a homodimer mediated by its carboxyl domain. We show here that a conserved motif exists within the carboxyl domain. A high resolution crystal structure and solution NMR structures of this motif reveal a novel and stable helical dimerization domain. We additionally determined a solution NMR structure of a divergent fungal homolog, and comparison of these structures allows annotation of specific stabilizing interactions. Using solution x-ray scattering and the structures of all folded domains, we present a model of the full-length Get4/Get5 complex.

SUBMITTER: Chartron JW

PROVIDER: S-EPMC3318709 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature

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Get5 carboxyl-terminal domain is a novel dimerization motif that tethers an extended Get4/Get5 complex.

Chartron Justin W JW VanderVelde David G DG Rao Meera M Clemons William M WM

The Journal of biological chemistry 20120117 11

Tail-anchored trans-membrane proteins are targeted to membranes post-translationally. The proteins Get4 and Get5 form an obligate complex that catalyzes the transfer of tail-anchored proteins destined to the endoplasmic reticulum from Sgt2 to the cytosolic targeting factor Get3. Get5 forms a homodimer mediated by its carboxyl domain. We show here that a conserved motif exists within the carboxyl domain. A high resolution crystal structure and solution NMR structures of this motif reveal a novel ...[more]

PMID: 22262836

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