PMID- 10391904
OWN - NLM
STAT- MEDLINE
DCOM- 19990805
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 28
DP  - 1999 Jul 9
TI  - Identification and expression of the TREX1 and TREX2 cDNA sequences encoding
      mammalian 3'-->5' exonucleases.
PG  - 19655-60
AB  - The 3'-->5' exonucleases catalyze the excision of nucleoside monophosphates from 
      the 3' termini of DNA. We have identified the cDNA sequences encoding two 3'-->5'
      exonucleases (TREX1 and TREX2) from mammalian cells. The TREX1 and TREX2 proteins
      are 304 and 236 amino acids in length, respectively. Analysis of the TREX1 and
      TREX2 sequences identifies three conserved motifs that likely generate the
      exonuclease active site in these enzymes. The specific amino acids in these three
      conserved motifs suggest that these mammalian exonucleases are most closely
      related to the proofreading exonucleases of the bacterial replicative DNA
      polymerases and the RNase T enzymes. Expression of TREX1 and TREX2 in Escherichia
      coli demonstrates that these recombinant proteins are active 3'-->5'
      exonucleases. The recombinant TREX1 protein was purified, and exonuclease
      activity was measured using single-stranded, partial duplex, and mispaired
      oligonucleotide DNA substrates. The greatest activity of the TREX1 protein was
      detected using a partial duplex DNA containing five mispaired nucleotides at the 
      3' terminus. No activity was detected using single-stranded RNA or an RNA-DNA
      partial duplex. Identification of the TREX1 and TREX2 cDNA sequences provides the
      genetic tools to investigate the physiological roles of these exonucleases in
      mammalian DNA replication, repair, and recombination pathways.
FAU - Mazur, D J
AU  - Mazur DJ
AD  - Wake Forest University School of Medicine, Department of Biochemistry,
      Winston-Salem, North Carolina 27157, USA.
FAU - Perrino, F W
AU  - Perrino FW
LA  - eng
SI  - GENBANK/AF151105
SI  - GENBANK/AF151106
SI  - GENBANK/AF151107
SI  - GENBANK/AF151108
GR  - CA12197/CA/NCI NIH HHS/United States
GR  - CA75350/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Recombinant Proteins)
RN  - EC 3.1.- (Exodeoxyribonucleases)
RN  - EC 3.1.11.5 (Exodeoxyribonuclease V)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cattle
MH  - Cloning, Molecular
MH  - DNA Repair
MH  - DNA Replication
MH  - DNA, Complementary/*genetics
MH  - Escherichia coli
MH  - Exodeoxyribonuclease V
MH  - Exodeoxyribonucleases/chemistry/*genetics
MH  - Gene Expression
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Recombinant Proteins/genetics
MH  - Recombination, Genetic
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
EDAT- 1999/07/03 00:00
MHDA- 1999/07/03 00:01
CRDT- 1999/07/03 00:00
PHST- 1999/07/03 00:00 [pubmed]
PHST- 1999/07/03 00:01 [medline]
PHST- 1999/07/03 00:00 [entrez]
AID - 10.1074/jbc.274.28.19655 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Jul 9;274(28):19655-60. doi: 10.1074/jbc.274.28.19655.