TY - JOUR
T1 - Characterization of AMA, a new AAA protein from Archaeoglobus and methanogenic archaea
AU - Djuranovic, Sergej
AU - Rockel, Beate
AU - Lupas, Andrei N.
AU - Martin, Jörg
PY - 2006/10
Y1 - 2006/10
N2 - 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.
AB - 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.
KW - AAA proteins
KW - AMA proteins
KW - ATPase
KW - Archaeoglobus fulgidus
KW - Chaperone activity
UR - http://www.scopus.com/inward/record.url?scp=33749252515&partnerID=8YFLogxK
U2 - 10.1016/j.jsb.2006.03.010
DO - 10.1016/j.jsb.2006.03.010
M3 - Article
C2 - 16730457
AN - SCOPUS:33749252515
SN - 1047-8477
VL - 156
SP - 130
EP - 138
JO - Journal of Structural Biology
JF - Journal of Structural Biology
IS - 1
ER -