PMID- 10558878
OWN - NLM
STAT- MEDLINE
DCOM- 19991220
LR  - 20061115
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 265
IP  - 2
DP  - 1999 Nov 19
TI  - Cloning of a cDNA encoding a rat DNase II-like acid DNase.
PG  - 395-9
AB  - DNase II is a well-known deoxyribonuclease (DNase) that catalyzes the hydrolysis 
      of DNA into oligonucleotides under acidic conditions. We have identified a novel 
      DNase that shows homology to DNase II, named DLAD, from a search of an expressed 
      sequence tag data base. The full-length cDNA for rat DLAD cloned by polymerase
      chain reaction encodes a 356-amino acid polypeptide containing a putative
      N-terminal signal peptide and 5 potential N-glycosylation sites; there is a
      predicted catalytic domain resemblance to rat DNase II. The predicted DLAD
      translation product shares 32.9% identity with DNase II. Interestingly,
      expression of the DRAD mRNA is highly restricted to the liver. A Myc-His tagged
      recombinant DLAD recovered mainly from the cytoplasm of transfected HeLa S3 cells
      has a divalent cation-independent DNase activity. The DLAD activity prefers
      acidic conditions to neutral. The recombinant protein expressed in HeLa S3 cells 
      inhibits the expression of GFP- and lac Z-expression vectors, suggesting that
      DLAD may play a role in elimination of exogenous DNA. Identification of the
      full-length cDNA for DLAD would lead to an understanding of the physiology of
      this DNase II-like molecule.
CI  - Copyright 1999 Academic Press.
FAU - Tanuma, S
AU  - Tanuma S
AD  - Department of Biochemistry, Faculty of Pharmaceutical Sciences, Science
      University of Tokyo, Japan. tanuma@ps.kagu.sut.ac.jp
FAU - Shiokawa, D
AU  - Shiokawa D
LA  - eng
SI  - GENBANK/AF178974
SI  - GENBANK/AF178975
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (DNA Primers)
RN  - 0 (DNA, Complementary)
RN  - 0 (Luminescent Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Proteins)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - EC 3.1.- (Deoxyribonucleases)
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  - Cloning, Molecular
MH  - DNA Primers/genetics
MH  - DNA, Complementary/*genetics
MH  - Deoxyribonucleases/*genetics
MH  - Endodeoxyribonucleases/genetics
MH  - Expressed Sequence Tags
MH  - Gene Expression
MH  - Green Fluorescent Proteins
MH  - HeLa Cells
MH  - Humans
MH  - Lac Operon
MH  - Luminescent Proteins/genetics
MH  - Molecular Sequence Data
MH  - RNA, Messenger/genetics/metabolism
MH  - Rats
MH  - Recombinant Proteins/genetics
MH  - Sequence Homology, Amino Acid
MH  - Transfection
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - 10.1006/bbrc.1999.1699 [doi]
AID - S0006291X99916996 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Nov 19;265(2):395-9. doi:
      10.1006/bbrc.1999.1699.