Some amino acids of the Pseudomonas aeruginosa MutL D(Q/M)HA(X)(2)E(X)(4)E conserved motif are essential for the in vivo function of the protein but not for the in vitro endonuclease activity.

Abstract excerpt

Human and Saccharomyces cerevisiae MutLα, and some bacterial MutL proteins, possess a metal ion-dependent endonuclease activity which is important for the in vivo function of these proteins. Conserved amino acids of the C-terminal region of human PMS2, S. cerevisiae PMS1 and of some bacterial MutL proteins have been implicated in the metal-binding/endonuclease activity. However, the contribution of individual...

Topics

• Amino Acid Motifs
• Amino Acid Sequence
• Conserved Sequence
• Endonucleases
• Models, Molecular
• Molecular Sequence Data
• Mutation
• Protein Conformation
• Pseudomonas aeruginosa
• Sequence Alignment