Purification and characterization of the nuclease NucM of Erwinia chrysanthemi.
The major periplasmic nuclease of Erwinia chrysanthemi strain 3937, NucM, has been purified near to homogeneity by a one step purification procedure, using chromatography on a sulfopropyl column. NucM cleaves randomly single and double-stranded DNA and RNA. It does not need divalent cations for its action, and is more active in low salt buffers. A serine and a histidine residue could be present in the catalytic site. Formation of disulfide bonds is necessary for NucM activity. NucM is probably synthesized as a reduced inactive polypeptide and becomes active in the periplasm once disulfide bonds are formed.
Moulard
M
M
Laboratoire de Génétique Moléculaire des Microorganismes et des Interactions Cellulaires, URA CNRS 1486, Institut National des Sciences Appliquées, Villeurbanne, France.
Condemine
G
G
Nasser
W
W
Robert-Baudouy
J
J
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D003851:Deoxyribonucleases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification*; D016974:Dickeya chrysanthemi / Q000201:enzymology*; D008969:Molecular Sequence Data; D013379:Substrate Specificity
D001426:Bacterial Proteins; D003851:Deoxyribonucleases; C082158:nucM protein, Erwinia chrysanthemi