PMID: 9079906Apr 1, 1997Paper

Purification and characterization of Mycoplasma penetrans Ca2+/Mg2+-dependent endonuclease

Journal of Bacteriology
M BendjennatE Bahraoui

Abstract

The major nuclease from Mycoplasma penetrans has been purified to homogeneity. The enzyme seems to be present as a membrane-associated precursor of 50 kDa and as a peripheral membrane monomeric polypeptide of 40 kDa that is easily removed by washing of cells with isotonic buffers and in the aqueous phase upon Triton partitioning of Triton X-114-solubilized protein. The 40-kDa nuclease was extracted from M. penetrans cells by Triton X-114 and phase fractionation and was further purified by chromatography on Superdex 75 and chelating Sepharose (Zn2+ form) columns. By gel filtration, the apparent molecular mass was 40 kDa. The purified enzyme exhibits both a nicking activity on superhelical and linear double-stranded DNA and a nuclease activity on RNA and single-stranded DNA. No exonuclease activity was found for this enzyme. This nuclease required both Mg2+ (optimum, 5 mM) and Ca2+ (optimum, 2 mM) for activity and exhibited a pH optimum between pH 7 and 8 for DNase activity. It was inhibited by Zn2+, Mn2+, heparin, sodium dodecyl sulfate, and chelator agents such EDTA and EGTA, but no effect was observed with ATP, 2-mercaptoethanol, N-ethylmaleimide, dithiothreitol, nonionic detergents, phenylmethylsulfonyl fluoride, and iodoacet...Continue Reading

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Citations

Dec 18, 1998·The Journal of Biological Chemistry·A UrbanoF Foss
Sep 10, 2019·Frontiers in Microbiology·Lianmei QinXiaoxing You
Jan 11, 2012·Nucleic Acid Therapeutics·Frank J HernandezJames O McNamara
Aug 24, 1999·Infection and Immunity·M BendjennatE Bahraoui
Aug 5, 2009·Infection and Immunity·Coreen JohnsonJoel B Baseman
Aug 24, 1999·Infection and Immunity·L Y Gao, Y Abu Kwaik
Dec 5, 1998·Microbiology and Molecular Biology Reviews : MMBR·S RazinY Naot

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