PMID- 10497274
OWN - NLM
STAT- MEDLINE
DCOM- 19991217
LR  - 20190501
IS  - 1362-4962 (Electronic)
IS  - 0305-1048 (Linking)
VI  - 27
IP  - 20
DP  - 1999 Oct 15
TI  - DLAD, a novel mammalian divalent cation-independent endonuclease with homology to
      DNase II.
PG  - 4083-9
AB  - In this report, we describe the molecular cloning and characterization of DLAD, a
      novel mammalian deoxy-ribonuclease homologous to DNase II. The full length cDNA
      for mouse DLAD has been cloned by polymerase chain reaction. The cDNA contains a 
      1065 bp open reading frame (ORF) encoding a 354 amino acid protein with a
      calculated molecular mass of 40 767. The predicted protein for DLAD shares 34.4% 
      identity with DNase II. DLAD is also homologous to three predicted proteins,
      C07B5.5, F09G8.2 and K04H4.6, from the nematode Caenorhabditis elegans.
      Furthermore, the third ORF of the fowlpox virus genome is found to encode a DLAD 
      homologue showing 37. 1% identity at the amino acid level. Northern blot analysis
      reveals that expression of the DLAD mRNA is highly restricted to the liver. DLAD 
      mainly exists as a cytoplasmic protein with divalent cation-independent
      endonuclease activity and cleaves DNA to produce 3'-phosphoryl/5'-hydroxyl ends. 
      It is active under a wide range of pH with maximum activity at pH 5.2. Among
      known DNase inhibitors tested, aurintricarboxylic acid and Zn(2+)are found to be 
      effective inhibitors of the DLAD activity.
FAU - Shiokawa, D
AU  - Shiokawa D
AD  - Department of Biochemistry, Faculty of Pharmaceutical Sciences, Science
      University of Tokyo, 12 Funagawara-machi, Ichigaya, Shinjuku-ku, Tokyo 162-0826, 
      Japan.
FAU - Tanuma, S
AU  - Tanuma S
LA  - eng
SI  - GENBANK/AF128888
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Nucleic Acids Res
JT  - Nucleic acids research
JID - 0411011
RN  - 0 (Cations, Divalent)
RN  - 0 (DNA, Complementary)
RN  - 9007-49-2 (DNA)
RN  - EC 3.1.- (Endodeoxyribonucleases)
RN  - EC 3.1.22.1 (deoxyribonuclease II)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cations, Divalent/metabolism
MH  - Cloning, Molecular
MH  - DNA/metabolism
MH  - DNA, Complementary/chemistry/isolation & purification
MH  - Endodeoxyribonucleases/chemistry/*genetics/*metabolism
MH  - Expressed Sequence Tags
MH  - HeLa Cells
MH  - Humans
MH  - Hydrolysis
MH  - Mice
MH  - Molecular Sequence Data
PMC - PMC148677
EDAT- 1999/09/25 00:00
MHDA- 1999/09/25 00:01
CRDT- 1999/09/25 00:00
PHST- 1999/09/25 00:00 [pubmed]
PHST- 1999/09/25 00:01 [medline]
PHST- 1999/09/25 00:00 [entrez]
AID - gkc604 [pii]
AID - 10.1093/nar/27.20.4083 [doi]
PST - ppublish
SO  - Nucleic Acids Res. 1999 Oct 15;27(20):4083-9. doi: 10.1093/nar/27.20.4083.