Characterization of AMA, a new AAA protein from Archaeoglobus and methanogenic archaea.
J Struct Biol
; 156(1): 130-8, 2006 Oct.
Article
em En
| MEDLINE
| ID: mdl-16730457
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.
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Base de dados:
MEDLINE
Assunto principal:
Archaea
/
Adenosina Trifosfatases
/
Archaeoglobus
/
Proteínas Arqueais
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article