PMID- 10452521
OWN - NLM
STAT- MEDLINE
DCOM- 19990909
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 456
IP  - 1
DP  - 1999 Jul 30
TI  - Molecular cloning and functional expression of a human peptide methionine
      sulfoxide reductase (hMsrA).
PG  - 17-21
AB  - Oxidation of methionine residues in proteins to methionine sulfoxide can be
      reversed by the enzyme peptide methionine sulfoxide reductase (MsrA, EC 1.8.4.6).
      We cloned the gene encoding a human homologue (hMsrA) of the enzyme, which has an
      88% amino acid sequence identity to the bovine version (bMsrA). With dot blot
      analyses based on RNA from human tissues, expression of hMsrA was found in all
      tissues tested, with highest mRNA levels in adult kidney and cerebellum, followed
      by liver, heart ventricles, bone marrow and hippocampus. In fetal tissue,
      expression was highest in the liver. No expression of hmsrA was detected in
      leukemia and lymphoma cell lines. To test if hMsrA is functional in cells, we
      assayed its effect on the inactivation time course of the A-type potassium
      channel ShC/B since this channel property strongly depends on the oxidative state
      of a methionine residue in the N-terminal part of the polypeptide. Co-expression 
      of ShC/B and hMsrA in Xenopus oocytes significantly accelerated inactivation,
      showing that the cloned enzyme is functional in an in vivo assay system.
      Furthermore, the activity of a purified glutathione-S-transferase-hMsrA fusion
      protein was demonstrated in vitro by measuring the reduction of [3H]N-acetyl
      methionine sulfoxide.
FAU - Kuschel, L
AU  - Kuschel L
AD  - Arbeitsgruppe Molekulare und zellulare Biophysik, Klinikum der
      Friedrich-Schiller-Universitat Jena, Germany.
FAU - Hansel, A
AU  - Hansel A
FAU - Schonherr, R
AU  - Schonherr R
FAU - Weissbach, H
AU  - Weissbach H
FAU - Brot, N
AU  - Brot N
FAU - Hoshi, T
AU  - Hoshi T
FAU - Heinemann, S H
AU  - Heinemann SH
LA  - eng
SI  - GENBANK/AJ242973
GR  - GM 57654/GM/NIGMS 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  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Potassium Channels)
RN  - 0 (Recombinant Fusion Proteins)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.8.4.- (Methionine Sulfoxide Reductases)
RN  - EC 1.8.4.11 (methionine sulfoxide reductase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cell Line/enzymology
MH  - Cerebellum/enzymology
MH  - Cloning, Molecular
MH  - Enzyme Activation
MH  - Female
MH  - Fetus/enzymology
MH  - Gene Expression Regulation, Developmental
MH  - Humans
MH  - Kidney/enzymology/growth & development
MH  - Leukemia/enzymology
MH  - Liver/embryology/enzymology
MH  - Lung/enzymology
MH  - Lymphoma/enzymology
MH  - Methionine Sulfoxide Reductases
MH  - Molecular Sequence Data
MH  - Myocardium/enzymology
MH  - Oocytes/enzymology
MH  - Oxidoreductases/*genetics/*metabolism
MH  - Potassium Channels/metabolism
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Xenopus laevis
EDAT- 1999/08/19 00:00
MHDA- 1999/08/19 00:01
CRDT- 1999/08/19 00:00
PHST- 1999/08/19 00:00 [pubmed]
PHST- 1999/08/19 00:01 [medline]
PHST- 1999/08/19 00:00 [entrez]
AID - S0014-5793(99)00917-5 [pii]
AID - 10.1016/s0014-5793(99)00917-5 [doi]
PST - ppublish
SO  - FEBS Lett. 1999 Jul 30;456(1):17-21. doi: 10.1016/s0014-5793(99)00917-5.