The hSNM1 protein is a DNA 5'-exonuclease.
The human SNM1 protein is a member of a highly conserved group of proteins catalyzing the hydrolysis of nucleic acid substrates. Although overproduction is unstable in mammalian cells, we have overproduced a recombinant hSNM1 protein in an insect cell system. The protein is a single-strand 5'-exonuclease, like its yeast homolog. The enzyme utilizes either DNA or RNA substrates, requires a 5'-phosphate moiety, shows very little activity on double-strand substrates, and functions at a size consistent with a monomer. The exonuclease activity requires the conserved beta-lactamase domain; site-directed mutagenesis of a conserved aspartate inactivates the exonuclease.
Hejna
James
J
Oregon Health & Science University, Department of Molecular and Medical Genetics, 3181 SW Sam Jackson Park Road, Mail Code L103, Portland, OR 97239-3098, USA.
Philip
Sahaayaruban
S
Ott
Jesse
J
Faulkner
Craig
C
Moses
Robb
R
D000818:Animals; D001224:Aspartic Acid / Q000235:genetics; D002460:Cell Line; D045643:DNA Repair Enzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000378:metabolism; D004331:Drosophila melanogaster / Q000166:cytology; D004706:Endodeoxyribonucleases / Q000378:metabolism; D005090:Exodeoxyribonucleases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D016297:Mutagenesis, Site-Directed; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism