Abstract:
:Polymerase gamma, which replicates and repairs mitochondrial DNA, requires the Pol gamma B subunit for processivity. We determined the crystal structure of mouse Pol gamma B, a core component of the mitochondrial replication machinery. Pol gamma B shows high similarity to glycyl-tRNA synthetase and dimerizes through an unusual intermolecular four-helix bundle. A human Pol gamma B mutant lacking the four-helix bundle failed to dimerize in solution or to stimulate the catalytic subunit Pol gamma A, but retained the ability to bind with Pol gamma A to a primer-template construct, indicating that the functional holoenzyme contains two Pol gamma B molecules. Other mutants retained stimulatory activity but lost the ability to bind folded ssDNA. These results suggest that the Pol gamma B dimer contains distinct sites for Pol gamma A binding, dimerization, and DNA binding.
journal_name
Mol Celljournal_title
Molecular cellauthors
Carrodeguas JA,Theis K,Bogenhagen DF,Kisker Cdoi
10.1016/s1097-2765(01)00153-8subject
Has Abstractpub_date
2001-01-01 00:00:00pages
43-54issue
1eissn
1097-2765issn
1097-4164pii
S1097-2765(01)00153-8journal_volume
7pub_type
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