Artículos
Título:
Analysis of the interaction interfaces of the N-terminal domain from Pseudomonas aeruginosa MutL
Autor/es:
MIGUEL, V.; CORREA, E. M. E.; DE TULLIO, L.; BARRA, J. L.; ARGARAÑA, C. E.; VILLAREAL, M. A.
Editorial:
PUBLIC LIBRARY SCIENCE
Referencias:
Lugar: San Francisco; Año: 2013 p. 1 - 1
Resumen:
bstract
Mismatch Repair System corrects mutations arising from DNA replication that escape from DNA polymerase proofreading
activity. This system consists of three main proteins, MutS-L-H, responsible for lesion recognition and repair. MutL is a
member of GHKL ATPase family and its ATPase cycle has been proposed to modulate MutL activity during the repair
process. Pseudomonas aeruginosa MutL (PaMutL) contains an N-terminal (NTD) ATPase domain connected by a linker to a Cterminal
(CTD) dimerization domain that possesses metal ion-dependent endonuclease activity. With the aim to identify
characteristics that allow the PaMutL NTD allosteric control of CTD endonuclease activity, we used an in silico and
experimental approach to determine the interaction surfaces of P. aeruginosa NTD (PaNTD), and compared it with the well
characterized Escherichia coli MutL NTD (EcNTD). Molecular dynamics simulations of PaNTD and EcNTD bound to or free of
adenosine nucleotides showed that a signif