the c-terminal domain of the mutl homolog from neisseria gonorrhoeae forms an inverted homodimerc端域mutl同系物的淋球菌倒置的为形式.pdfVIP

The C-Terminal Domain of the MutL Homolog from Neisseria gonorrhoeae Forms an Inverted Homodimer 1. 1. 2. 2 3 Sivakumar Namadurai , Deepti Jain , Dhananjay S. Kulkarni , Chaitanya R. Tabib , Peter Friedhoff , 2 1 Desirazu N. Rao , Deepak T. Nair * ¨ 1 Laboratory 4, National Centre for Biological Sciences, Bangalore, India, 2 Department of Biochemistry, Indian Institute of Science, Bangalore, India, 3 Institut fur ¨ Biochemie (FB 08), Justus-Liebig-Universitat, Giessen, Germany Abstract The mismatch repair (MMR) pathway serves to maintain the integrity of the genome by removing mispaired bases from the newly synthesized strand. In E. coli, MutS, MutL and MutH coordinate to discriminate the daughter strand through a mechanism involving lack of methylation on the new strand. This facilitates the creation of a nick by MutH in the daughter strand to initiate mismatch repair. Many bacteria and eukaryotes, including humans, do not possess a homolog of MutH. Although the exact strategy for strand discrimination in these organisms is yet to be ascertained, the required nicking endonuclease activity is resident in the C-terminal domain of MutL. This activity is dependent on the integrity of a conserved metal binding motif. Unlike their eukaryotic counterparts, MutL in bacteria like Neisseria exist in the form of a homodimer. Even thou