Disulfide bonds are required for Serratia marcescens nuclease activity.
The role of the two disulfide bonds found in the Serratia marcescens nuclease were tested by site directed mutagenesis and were found essential for nuclease activity, although slight residual activity remained. The requirement for disulfide bond formation may play a role in preventing the lethal action of nuclease while in the bacterial cytoplasm.
Ball
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TK
Department of Biochemical and Biophysical Sciences, University of Houston, TX 77204-5934.
Suh
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Benedik
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MJ
D000483:Alleles; D015153:Blotting, Western; D003001:Cloning, Molecular; D003545:Cysteine; D004220:Disulfides; D004706:Endodeoxyribonucleases; D004720:Endonucleases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004722:Endoribonucleases; D005798:Genes, Bacterial; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D012706:Serratia marcescens / Q000201:enzymology* / Q000235:genetics
D004220:Disulfides; D011994:Recombinant Proteins; D004706:Endodeoxyribonucleases; D004720:Endonucleases; D004722:Endoribonucleases; C021835:Serratia marcescens nuclease; D003545:Cysteine