PMID- 15317934
OWN - NLM
STAT- MEDLINE
DCOM- 20041116
LR  - 20181113
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 101
IP  - 35
DP  - 2004 Aug 31
TI  - Identification and characterization of phosphoseryl-tRNA[Ser]Sec kinase.
PG  - 12848-53
AB  - In 1970, a kinase activity that phosphorylated a minor species of seryl-tRNA to 
      form phosphoseryl-tRNA was found in rooster liver [Maenpaa, P. H. & Bernfield, M. 
      R. (1970) Proc. Natl. Acad. Sci. USA 67, 688-695], and a minor seryl-tRNA that 
      decoded the nonsense UGA was detected in bovine liver. The phosphoseryl-tRNA and 
      the minor UGA-decoding seryl-tRNA were subsequently identified as selenocysteine 
      (Sec) tRNA[Ser]Sec, but the kinase activity remained elusive. Herein, by using a 
      comparative genomics approach that searched completely sequenced archaeal genomes 
      for a kinase-like protein with a pattern of occurrence similar to that of 
      components of Sec insertion machinery, we detected a candidate gene for mammalian 
      phosphoseryl-tRNA[Ser]Sec kinase (pstk). Mouse pstk was cloned, and the gene 
      product (PSTK) was expressed and characterized. PSTK specifically phosphorylated 
      the seryl moiety on seryl-tRNA[Ser]Sec and, in addition, had a requirement for 
      ATP and Mg2+. Proteins with homology to mammalian PSTK occur in Drosophila, 
      Caenorhabditis elegans, Methanopyrus kandleri, and Methanococcus jannaschii, 
      suggesting a conservation of its function across archaea and eukaryotes that 
      synthesize selenoproteins and the absence of this function in bacteria, plants, 
      and yeast. The fact that PSTK has been highly conserved in evolution suggests 
      that it plays an important role in selenoprotein biosynthesis and/or regulation.
CI  - Copyright 2004 The National Academy of Sciencs of the USA
FAU - Carlson, Bradley A
AU  - Carlson BA
AD  - Molecular Biology of Selenium Section, Laboratory of Cancer Prevention, Center 
      for Cancer Research, National Cancer Institute, National Institutes of Health, 
      Bethesda, MD 20892, USA.
FAU - Xu, Xue-Ming
AU  - Xu XM
FAU - Kryukov, Gregory V
AU  - Kryukov GV
FAU - Rao, Mahadev
AU  - Rao M
FAU - Berry, Marla J
AU  - Berry MJ
FAU - Gladyshev, Vadim N
AU  - Gladyshev VN
FAU - Hatfield, Dolph L
AU  - Hatfield DL
LA  - eng
GR  - R01 GM061603/GM/NIGMS NIH HHS/United States
GR  - GM061603/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20040818
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (RNA, Transfer, Amino Acyl)
RN  - 0 (RNA, Transfer, Ser)
RN  - 0 (selenocysteinyl-tRNA)
RN  - EC 2.7.- (Phosphotransferases)
SB  - IM
CIN - Proc Natl Acad Sci U S A. 2004 Sep 14;101(37):13395-6. PMID: 15353586
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Computational Biology
MH  - Molecular Sequence Data
MH  - Phosphorylation
MH  - Phosphotransferases/*chemistry/isolation & purification/metabolism
MH  - RNA, Transfer, Amino Acyl/*metabolism
MH  - RNA, Transfer, Ser/*metabolism
PMC - PMC516484
EDAT- 2004/08/20 05:00
MHDA- 2004/11/17 09:00
PMCR- 2005/02/28
CRDT- 2004/08/20 05:00
PHST- 2004/08/20 05:00 [pubmed]
PHST- 2004/11/17 09:00 [medline]
PHST- 2004/08/20 05:00 [entrez]
PHST- 2005/02/28 00:00 [pmc-release]
AID - 0402636101 [pii]
AID - 10112848 [pii]
AID - 10.1073/pnas.0402636101 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12848-53. doi: 
      10.1073/pnas.0402636101. Epub 2004 Aug 18.