The role of MutS oligomers on Pseudomonas aeruginosa Mismatch Repair System activity

MONTI MARIELA R.*; MIGUEL VIRGINIA*; ARGARAÑA CARLOS E.; CO-AUTORAS

DNA REPAIR

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2008 vol. 7 p. 1799 - 1799

1568-7864

he Escherichia coli DNA Mismatch Repair (MMR) protein MutS exist as dimers and tetramers in solution, and the identification of its functional oligomeric state has been matter of extensive study. In the present work, we have analyzed the oligomerization state of MutS from Pseudomonas aeruginosa a bacterial species devoid of Dam methylation and MutH homologue. By analyzing native MutS and different mutated versions of the protein, we determined that P. aeruginosa MutS is mainly tetrameric in solution and that its oligomerization capacity is conducted as in E. coli, by the C-terminal region of the protein. The analysis of mismatch oligonucleotide binding activity showed that wild-type MutS binds to DNA as tetramer. The DNA binding activity decreased when the C-terminal region was deleted (MutS <!-- /* Font Definitions */ @font-face {font-family:"Pala