PMID- 10500251
OWN - NLM
STAT- MEDLINE
DCOM- 19991105
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1447
IP  - 1
DP  - 1999 Oct 6
TI  - cDNA cloning, expression and chromosomal localization of the mouse mitochondrial 
      thioredoxin reductase gene(1).
PG  - 113-8
AB  - Cytosolic thioredoxin (Trx) and thioredoxin reductase (TrxR) comprise a
      ubiquitous system that uses the reducing power of NADPH to act as a general
      disulfide reductase system as well as a potent antioxidant system. Human and rat 
      mitochondria contain a complete thioredoxin system different from the one present
      in the cytosol. The mitochondrial system is involved in the oxidative stress
      protection through a mitochondrial thioredoxin-dependent peroxidase. We report
      here the cDNA cloning and chromosomal localization of the mouse mitochondrial
      thioredoxin reductase gene (TrxR2). The mouse TrxR2 cDNA encodes for a putative
      protein of 527 amino acid residues with a calculated molecular mass of 57 kDa,
      that displays high homology with the human and rat counterparts. The N-terminus
      of the protein displays typical features of a mitochondrial targeting sequence
      with absence of acidic residues and abundance of basic residues. Mouse TrxR2 also
      contains a stop codon in frame at the C-terminus of the protein, necessary for
      the incorporation of selenocysteine that is required for enzymatic activity. The 
      typical stem-loop structure (SECIS element) that drives the incorporation of
      selenocysteine is identified in the 3'-UTR. Northern analysis of the mouse TrxR2 
      mRNA shows a similar pattern of expression with the human homologue, with higher 
      expression in liver, heart and kidney. Finally, we have assigned the mouse TrxR2 
      gene to chromosome 16 mapping at 11.2 cM from the centromer and linked to the
      catechol-o-methyltransferase (comt) gene.
FAU - Miranda-Vizuete, A
AU  - Miranda-Vizuete A
AD  - Department of Biosciences, Center for Biotechnology, Karolinska Institutet,
      Novum, S-141 57, Huddinge, Sweden.
FAU - Damdimopoulos, A E
AU  - Damdimopoulos AE
FAU - Spyrou, G
AU  - Spyrou G
LA  - eng
SI  - GENBANK/AF136399
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (DNA, Complementary)
RN  - EC 1.8.1.9 (Thioredoxin-Disulfide Reductase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - DNA, Complementary/chemistry
MH  - Gene Expression
MH  - Kidney/metabolism
MH  - Male
MH  - Mice
MH  - Mitochondria/*enzymology
MH  - Mitochondria, Heart/metabolism
MH  - Mitochondria, Liver/metabolism
MH  - Molecular Sequence Data
MH  - Sequence Alignment
MH  - Testis/metabolism
MH  - Thioredoxin-Disulfide Reductase/chemistry/*genetics
EDAT- 1999/09/29 00:00
MHDA- 1999/09/29 00:01
CRDT- 1999/09/29 00:00
PHST- 1999/09/29 00:00 [pubmed]
PHST- 1999/09/29 00:01 [medline]
PHST- 1999/09/29 00:00 [entrez]
AID - S0167478199001293 [pii]
AID - 10.1016/s0167-4781(99)00129-3 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Oct 6;1447(1):113-8. doi:
      10.1016/s0167-4781(99)00129-3.