Noncatalytic aspartate at the exonuclease domain of proofreading DNA polymerases regulates both degradative and synthetic activities.

ABSTRACT: Most replicative DNA polymerases (DNAPs) are endowed with a 3'-5' exonuclease activity to proofread the polymerization errors, governed by four universally conserved aspartate residues belonging to the Exo I, Exo II, and Exo III motifs. These residues coordinate the two metal ions responsible for the hydrolysis of the last phosphodiester bond of the primer strand. Structural alignment of the conserved exonuclease domain of DNAPs from families A, B, and C has allowed us to identify an additional and invariant aspartate, located between motifs Exo II and Exo III. The importance of this aspartate has been assessed by site-directed mutagenesis at the corresponding Asp¹²¹ of the family B ϕ29 DNAP. Substitution of this residue by either glutamate or alanine severely impaired the catal

SUBMITTER: Del Prado A 

PROVIDER: S-EPMC5879684 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature