Fragmentation of acetate-CoA ligase gives a clue to understand domain rearrangement history of NDP-forming acyl-CoA synthetase superfamily proteins.

Bioscience, Biotechnology, and Biochemistry
Yoko ChibaKen Takai

Abstract

NDP-forming type acyl-CoA synthetase superfamily proteins are known to have six essential subdomains (1, 2, 3, a, b, c) of which partition and order are varied, suggesting yet-to-be-defined subdomain rearrangement happened in its evolution. Comparison in physicochemical and biochemical characteristics between the recombinant proteins which we made from fragmented subdomains and wild-type protein, acetate-CoA ligase in a hyperthermophilic archaeon, consisting of two distinct subunits (α1-2-3 and βa-b-c) provided a clue to the mystery of its molecular evolutionary passage. Although solubility and thermostability of each fragmented subdomain turned out to be lower than that of wild-type, mixture of the three synthetic subunits of α1-2, α3, and βa-b-c had quaternary structure, thermostability, and enzymatic activity comparable to those of the wild-type. This suggests that substantial independence and mobility of subdomain 3 have enabled rearrangement of the subdomains; and thermostability of the subdomains has constrained the composition of the subunits.

References

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Mar 19, 2003·Journal of Theoretical Biology·Massimo Di Giulio
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Aug 27, 2016·Nature Microbiology·Madeline C WeissWilliam F Martin

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Datasets Mentioned

BETA
AAL64786.1

Methods Mentioned

BETA
gel-filtration
protein assay
size-exclusion chromatography

Software Mentioned

Blastp
Prime

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