SMANIA ANDREA
Artículos
Título:
Properties of MutS from Pseudomonas aeruginosa. Nucleotides and heteroduplex DNA preserve the active conformation of MutS by inhibition of protein aggregation
Autor/es:
PEZZA R.J.,; SMANIA A. M.; BARRA J.L.,; ARGARAÑA C.E.,
Editorial:
PORTLAND PRESS LTD
Referencias:
Año: 2002 vol. 361 p. 87 - 87
Resumen:
p style="MARGIN: 0cm 0cm 0pt; mso-layout-grid-align: none" class="MsoNormal">MutS, a component of the mismatch repair system begins the DNA reparation process by recognizing base}base mismatches or small insertion}deletion loops. We have cloned the mutS gene from the human opportunistic pathogen Pseudomonas aeruginosa and analysed the biochemical properties of the encoded protein. Complementation of the hypermutator phenotype of a P. aeruginosa mutS mutant strain indicated that the isolated gene was functional. When puri®ed MutS was incubated at 37 °C in the absence of ligands, a rapid inactivation of the oligonucleotide binding capability and ATPase activity occurred. However, the presence of ATP, ADP or heteroduplex oligonucleotides, but not homoduplex oligonucleotides, prevented the protein from being inactivated. The analysis of the protein by native PAGE indicated that the active conformation state corr