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Papers In Press, published online ahead of print December 21, 2000
Pharmacology, Univ Mass Medical School, Worcester, MA 01655
Corresponding Author: martin.marinus{at}umassmed.edu
Site-directed mutagenesis was performed on several areas of MutH based on the similarity of MutH and PvuII structural models. The aims were to identify DNA binding residues; to determine if MutH has the same mechanism for DNA binding and catalysis as PvuII; and to localize the residues responsible for MutH stimulation by MutL. No DNA binding residues were identified in the two flexible loop regions of MutH, although similar loops in PvuII are involved in DNA binding. Two histidines in MutH are in a similar position as two histidines (H84 and H85) in PvuII that signal for DNA binding and catalysis. These MutH histidines (H112 and H115) were changed to alanines, but the mutant proteins had wild-type activity both in-vivo and in-vitro. The results indicate that the MutH signal for DNA binding and catalysis remains unknown. Instead, a lysine residue (K48) was found in the first flexible loop that functions in catalysis together with the three presumed catalytic amino acids (Asp70, Glu77, and Lys79). Two deletion mutations (MutH
J. Biol. Chem, 10.1074/jbc.M007935200
Submitted on August 30, 2000
Revised on November 30, 2000
Accepted on December 20, 2000
Mutational analysis of the MutH protein from Escherichia coli
224 and MutH214) in the C-terminal end of the protein, localized the MutL stimulation region to five amino acids (Ala220, Leu221, Leu222, Ala223, and Arg224).
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