The Architecture of the Anbu Complex Reflects an Evolutionary Intermediate at 
the Origin of the Proteasome System

Fuchs, ACD; Alva, V; Maldoner, L; Albrecht, R; Hartmann, MD; Martin, J

doi:10.1016/j.str.2017.04.005

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The Architecture of the Anbu Complex Reflects an Evolutionary Intermediate at the Origin of the Proteasome System

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Fuchs, ACD
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Protein Folding, Unfolding and Degradation Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

/persons/resource/persons271574

Alva, V
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Protein Bioinformatics Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Maldoner, L
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Albrecht, R
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Hartmann, MD
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Martin, J
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Protein Folding, Unfolding and Degradation Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Fuchs, A., Alva, V., Maldoner, L., Albrecht, R., Hartmann, M., & Martin, J. (2017). The Architecture of the Anbu Complex Reflects an Evolutionary Intermediate at the Origin of the Proteasome System. Structure, 25(6), 834-845. doi:10.1016/j.str.2017.04.005.

Cite as: https://hdl.handle.net/21.11116/0000-0002-0383-6

Abstract

Proteasomes are self-compartmentalizing proteases that function at the core of the cellular protein degradation machinery in eukaryotes, archaea, and some bacteria. Although their evolutionary history is under debate, it is thought to be linked to that of the bacterial protease HsIV and the hypothetical bacterial protease Anbu (ancestral beta subunit). Here, together with an extensive bioinformatic analysis, we present the first biophysical characterization of Anbu. Anbu forms a dodecameric complex with a unique architecture that was only accessible through the combination of X-ray crystallography and small-angle X-ray scattering. While forming continuous helices in crystals and electron microscopy preparations, refinement of sections from the crystal structure against the scattering data revealed a helical open ring structure in solution, contrasting the ring shaped structures of proteasome and HsIV. Based on this primordial architecture and exhaustive sequence comparisons, we propose that Anbu represents an ancestral precursor at the origin of self compartmentalization.