Characterization of AMA, a new AAA protein from Archaeoglobus and methanogenic 
archaea

Djuranovic, S; Rockel, B; Lupas, AN; Martin, J

doi:10.1016/j.jsb.2006.03.010

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Characterization of AMA, a new AAA protein from Archaeoglobus and methanogenic archaea

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Djuranovic, S
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Lupas, AN
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

Djuranovic, S., Rockel, B., Lupas, A., & Martin, J. (2006). Characterization of AMA, a new AAA protein from Archaeoglobus and methanogenic archaea. Journal of Structural Biology, 156(1), 130-138. doi:10.1016/j.jsb.2006.03.010.

Cite as: https://hdl.handle.net/21.11116/0000-000B-284E-2

Abstract

We have previously reported a new group of AAA proteins, which is only found in Archaeoglobus and methanogenic archaea (AMA). The proteins are phylogenetically basal to the metalloprotease clade and their N-terminal domain is homologous to the beta-clam part of the N-domain of CDC48-like proteins. Here we report the biochemical and biophysical characterization of Archaeoglobus fulgidus AMA, and of its isolated N-terminal (AMA-N) and ATPase (AMA-DeltaN) domains. AfAMA forms hexameric complexes, as does AMA-N, while AMA-DeltaN only forms dimers. The ability to hexamerize is dependent on the integrity of a GYPL motif in AMA-N, which resembles the pore motif of FtsH and HslU. While the physiological function of AMA is unknown, we show that it has ATP-dependent chaperone activity and can prevent the thermal aggregation of proteins in vitro. The ability to interact with non-native proteins resides in the N-domain and is energy-independent.