Abstract
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.
MeSH Terms
Alleles
Blotting, Western
Cloning, Molecular
Cysteine
Disulfides
Endodeoxyribonucleases
Endonucleases/genetics,isolation & purification,metabolism
Endoribonucleases
Genes, Bacterial
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Plasmids
Recombinant Proteins/isolation & purification,metabolism
Serratia marcescens/enzymology,genetics
Chemicals
Disulfides
Recombinant Proteins
Endodeoxyribonucleases
Endonucleases
Endoribonucleases
Serratia marcescens nuclease
Cysteine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ball T K
Department of Biochemical and Biophysical Sciences, University of Houston, TX 77204-5934.
Suh Y
Benedik M J
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