PMID- 10049785
OWN - NLM
STAT- MEDLINE
DCOM- 19990401
LR  - 20120801
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 255
IP  - 3
DP  - 1999 Feb 24
TI  - Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced
      amino acid sequences in terms of the structural domains and coordinately
      regulated expression of the alpha and beta subunits in chronic myeloid leukemia
      cells.
PG  - 765-73
AB  - Unlike the catalytic alpha-subunit, the beta-subunit of heterodimeric
      (alphabeta)2 phenylalanyl-tRNA synthetase (PheRS) has no invariant functional
      amino acids directly involved in the aminoacylation process as it is evident from
      the crystal structure of the T. thermophilus enzyme complexed with tRNAPhe.
      Having no catalytic function, the prokaryotic beta-subunit comprises OB-, RNP-,
      SH3-, and DNA-binding-like domains involved in a variety of biological functions 
      in other proteins. It was shown that the mRNA of the human alpha-subunit
      overexpressed in the tumorigenic versus the nontumorigenic variant of the same
      acute-phase chronic myeloid leukemia cell line (CML). We cloned, sequenced, and
      expressed human PheRS. The layout of the human sequence indicates that the
      general tRNA binding mode and anticodon recognition differ between prokaryotes
      and eukaryotes for the phenylalanine system. Northern blot hybridization analysis
      from malignant and normal human tissues enabled us to assess the relative
      expression levels of the alpha- and beta-subunits independently, in view of the
      additional cellular role proposed for the beta-subunit in tumorigenic events. The
      levels of mRNA corresponding to the alpha- and beta-subunits were remarkably
      similar in all cell types and tissues examined, thus indicating the implication
      of the entire (alphabeta)2 heterodimer in tumorigenic events.
CI  - Copyright 1999 Academic Press.
FAU - Rodova, M
AU  - Rodova M
AD  - Department of Structural Biology, Weizmann Institute of Science, Rehovot, 76100, 
      Israel.
FAU - Ankilova, V
AU  - Ankilova V
FAU - Safro, M G
AU  - Safro MG
LA  - eng
SI  - GENBANK/AF042346
SI  - GENBANK/AF042347
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 (RNA, Messenger)
RN  - 0 (RNA, Neoplasm)
RN  - 0 (RNA, Transfer, Amino Acyl)
RN  - 0 (RNA-Binding Proteins)
RN  - EC 6.1.1.- (Amino Acyl-tRNA Synthetases)
SB  - IM
MH  - Amino Acyl-tRNA Synthetases/chemistry/*genetics
MH  - Animals
MH  - COS Cells
MH  - Cloning, Molecular
MH  - Dimerization
MH  - Gene Expression Regulation, Enzymologic/*genetics
MH  - Gene Expression Regulation, Neoplastic/genetics
MH  - Humans
MH  - Leukemia, Myeloid/*enzymology/genetics
MH  - RNA, Messenger/metabolism
MH  - RNA, Neoplasm/genetics
MH  - RNA, Transfer, Amino Acyl/*biosynthesis
MH  - RNA-Binding Proteins/chemistry/genetics
MH  - Sequence Alignment
MH  - Sequence Analysis, DNA
MH  - Transfection/genetics
MH  - Tumor Cells, Cultured
EDAT- 1999/03/02 00:00
MHDA- 1999/03/02 00:01
CRDT- 1999/03/02 00:00
PHST- 1999/03/02 00:00 [pubmed]
PHST- 1999/03/02 00:01 [medline]
PHST- 1999/03/02 00:00 [entrez]
AID - S0006-291X(99)90141-9 [pii]
AID - 10.1006/bbrc.1999.0141 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Feb 24;255(3):765-73. doi:
      10.1006/bbrc.1999.0141.