5 Scopus citations


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 β-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-ΔN) domains. AfAMA forms hexameric complexes, as does AMA-N, while AMA-ΔN 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.

Original languageEnglish
Pages (from-to)130-138
Number of pages9
JournalJournal of Structural Biology
Issue number1
StatePublished - Oct 2006


  • AAA proteins
  • AMA proteins
  • ATPase
  • Archaeoglobus fulgidus
  • Chaperone activity


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