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2017 ; 25
(6
): 834-845.e5
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The Architecture of the Anbu Complex Reflects an Evolutionary Intermediate at the
Origin of the Proteasome System
#MMPMID28479063
Fuchs ACD
; Alva V
; Maldoner L
; Albrecht R
; Hartmann MD
; Martin J
Structure
2017[Jun]; 25
(6
): 834-845.e5
PMID28479063
show ga
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 HslV 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 HslV. Based on this primordial
architecture and exhaustive sequence comparisons, we propose that Anbu represents
an ancestral precursor at the origin of self-compartmentalization.