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Unraveling the architecture of the A1 complex of the Nanoarchaeum equitans A1A0 ATP synthase
Author(s) -
Mohanty Soumya,
Hogue Christopher Warren Victor
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.999.3
Subject(s) - atp synthase , atp synthase gamma subunit , protein subunit , isothermal titration calorimetry , atpase , biology , biochemistry , hyperthermophile , archaea , enzyme , microbiology and biotechnology , atp hydrolysis , gene
ATP synthases are multimeric motors which are indispensible for cellular energetics. The archaeal ATP synthases are the oldest but are relatively understudied. Nanoarchaeum equitans is a nanosized parasitic hyperthermophile with several ancestral traits. Genomic annotation shows that the typical archaeal ATPase subunits are missing, suggesting that the N.equitans ATP synthase is either compromised or constructed partially. The annotated regulatory B subunit is shortened compared to the B subunits of other archaeal ATP synthases, which led to the speculation whether the A and B subunits are capable of forming a functional complex. This study aims at understanding the architecture and functionality of the catalytic A1 complex. The recombinant N. equitans ATPase subunits were purified, reconstituted in‐vitro and characterized using dynamic light scattering, size exclusion chromatography and Blue Native PAGE and isothermal titration calorimetry. Results show the stoichiometric association of A and the annotated smaller B subunits in the presence of nucleotides to form higher order complexes. Therefore our results suggest that the N.equitans ATP synthase might be a minimalistic, yet functional form which would provide a vital connection to the understanding of the evolution of ATP synthases. Supported by Mechanobiology Institute, National University of Singapore (Research Grant R714–009‐007–271)