PMID- 10329163
OWN - NLM
STAT- MEDLINE
DCOM- 19990609
LR  - 20131121
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 288
IP  - 4
DP  - 1999 May 14
TI  - Expression and characterization of a human mitochondrial phenylalanyl-tRNA
      synthetase.
PG  - 567-77
AB  - Human mitochondrial phenylalanyl-tRNA synthetase (mtPheRS) has been identified
      from the human EST database. Using consensus sequences derived from conserved
      regions of the alpha and beta-subunits from bacterial PheRS, two partially
      sequenced cDNA clones were identified. Unexpectedly, sequence analysis indicated 
      that one of these clones was a truncated form of the other. Detailed analysis
      indicates that unlike the (alphabeta)2 structure of the prokaryotic and
      eukaryotic cytoplasmic forms of PheRS, the human mtPheRS consists of a single
      polypeptide chain. This protein has been cloned and expressed in Escherichia
      coli. Gel filtration and analytical velocity sedimentation centrifugation
      indicate that the human mtPheRS is active in a monomeric form. The N-terminal 314
      amino acid residues appear to be analogous to the alpha-subunit of the
      prokaryotic PheRS, while the C-terminal 100 amino acid residues correspond to a
      region of the beta-subunit known to interact with the anticodon of tRNAPhe.
      Comparisons with the sequences of PheRS from yeast and Drosophila mitochondria
      indicate they are 42 % and 51 % identical with the human mtPheRS, respectively.
      Sequence analysis confirms the presence of motifs characteristic of class II
      aminoacyl-tRNA synthetases. KM and kcat values for ATP:PPi exchange and for the
      aminoacylation reaction carried out by human mtPheRS have been determined.
      Evolutionary origins of this small monomeric human mtPheRS are unknown, however, 
      implications are that this enzyme is a result of the simplification of the more
      complex (alphabeta)2 bacterial PheRS in which specific functional regions were
      retained.
CI  - Copyright 1998 Academic Press.
FAU - Bullard, J M
AU  - Bullard JM
AD  - Department of Chemistry, University of Texas Health Science Center, San Antonio, 
      TX, USA.
FAU - Cai, Y C
AU  - Cai YC
FAU - Demeler, B
AU  - Demeler B
FAU - Spremulli, L L
AU  - Spremulli LL
LA  - eng
SI  - GENBANK/AF097441
GR  - GM19117/GM/NIGMS NIH HHS/United States
GR  - GM32734/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (DNA, Complementary)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 6.1.1.20 (Phenylalanine-tRNA Ligase)
SB  - IM
MH  - Adenosine Triphosphate/metabolism
MH  - Amino Acid Sequence
MH  - Chromatography, Gel
MH  - DNA, Complementary
MH  - Humans
MH  - Mitochondria/*enzymology
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Phenylalanine-tRNA Ligase/chemistry/*genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Thermus/enzymology
MH  - Ultracentrifugation
EDAT- 1999/05/18 00:00
MHDA- 1999/05/18 00:01
CRDT- 1999/05/18 00:00
PHST- 1999/05/18 00:00 [pubmed]
PHST- 1999/05/18 00:01 [medline]
PHST- 1999/05/18 00:00 [entrez]
AID - S0022-2836(99)92708-0 [pii]
AID - 10.1006/jmbi.1999.2708 [doi]
PST - ppublish
SO  - J Mol Biol. 1999 May 14;288(4):567-77. doi: 10.1006/jmbi.1999.2708.