MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes.
We identify and characterize MlaA, a novel protein, which is found in a conserved operon with Mre11 and Rad50 in archaeal genomes. MlaA is fused with Mre11 in Methanobacter thermoautotrophicus, suggesting the MlaA is functionally linked to the Mre11 complex. MlaA preferentially and cooperatively binds double-stranded and secondary structure containing DNA and has double-stranded but not single-stranded DNA-stimulated ATPase activity. Electron microscopy reveals that MlaA forms a 360-kDa hexameric ring structure with a central hole. Our data suggest that the archaeal Mre11 complex is associated with a novel hexameric ATPase that could be required for the processing of DNA double-stranded breaks and recombination intermediates.
Manzan
Angelo
A
Gene Center, University of Munich, D-81377 Munich, Germany.
Pfeiffer
Günter
G
Hefferin
Melissa L
ML
Lang
Cara E
CE
Carney
James P
JP
Hopfner
Karl-Peter
KP
D000251:Adenosine Triphosphatases / Q000235:genetics*; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000235:genetics*; D004706:Endodeoxyribonucleases / Q000235:genetics*; D005090:Exodeoxyribonucleases / Q000235:genetics*; D020745:Genome, Archaeal; D008854:Microscopy, Electron; D008958:Models, Molecular; D008969:Molecular Sequence Data; D043903:Pyrococcus abyssi / Q000201:enzymology* / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D004706:Endodeoxyribonucleases; D005090:Exodeoxyribonucleases; C415985:Mre11 protein, archaeal; C415984:Rad50 protein, archaeal; D000251:Adenosine Triphosphatases