PMID- 11747308
OWN - NLM
STAT- MEDLINE
DCOM- 20020221
LR  - 20131121
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 397
IP  - 1
DP  - 2002 Jan 1
TI  - Maize seryl-tRNA synthetase: specificity of substrate recognition by the 
      organellar enzyme.
PG  - 40-50
AB  - In our study of seryl-tRNA formation in maize, we investigated the enzymes 
      involved in serylation. Only two dissimilar seryl-tRNA synthetase (SerRS) cDNA 
      clones were identified in the Zea mays EST (expressed sequence tag) databases. 
      One encodes a seryl-tRNA synthetase, which presumably functions in the organelles 
      (SerZMm), while the other synthetase product is more similar to eukaryotic 
      cytosolic counterparts (SerZMc). The expression of SerZMm in Saccharomyces 
      cerevisiae resulted in complementation of mutant respiratory phenotype, caused by 
      a disruption of the nuclear gene, presumably encoding yeast mitochondrial 
      seryl-tRNA synthetase (SerSCm). Purified mature SerZMm displays tRNA-assisted 
      serine activation and aminoacylates maize mitochondrial and chloroplast tRNA(Ser) 
      transcripts with similar efficiencies, raising the possibility that only two 
      isoforms of seryl-tRNA synthetase may be sufficient to catalyze seryl-tRNA(Ser) 
      formation in three cellular compartments of Zea mays. Phylogenetic analysis 
      suggests that SerZMm is of mitochondrial origin.
FAU - Rokov-Plavec, Jasmina
AU  - Rokov-Plavec J
AD  - Department of Chemistry, Faculty of Science, University of Zagreb, Strossmayerov 
      trg 14, 10000 Zagreb, Croatia.
FAU - Lesjak, Sonja
AU  - Lesjak S
FAU - Landeka, Irena
AU  - Landeka I
FAU - Mijakovic, Ivan
AU  - Mijakovic I
FAU - Weygand-Durasevic, Ivana
AU  - Weygand-Durasevic I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (DNA, Complementary)
RN  - 0 (Protein Isoforms)
RN  - 452VLY9402 (Serine)
RN  - 9014-25-9 (RNA, Transfer)
RN  - EC 6.1.1.11 (Serine-tRNA Ligase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Chloroplasts/metabolism
MH  - Cytosol/enzymology
MH  - DNA, Complementary/metabolism
MH  - Databases as Topic
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Evolution, Molecular
MH  - Expressed Sequence Tags
MH  - Genetic Complementation Test
MH  - Kinetics
MH  - Mitochondria/metabolism
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Nucleic Acid Conformation
MH  - Phenotype
MH  - Phylogeny
MH  - Protein Isoforms
MH  - RNA, Transfer/chemistry
MH  - Saccharomyces cerevisiae/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Serine/metabolism
MH  - Serine-tRNA Ligase/*chemistry
MH  - Substrate Specificity
MH  - Zea mays/*enzymology
EDAT- 2001/12/19 10:00
MHDA- 2002/02/22 10:01
CRDT- 2001/12/19 10:00
PHST- 2001/12/19 10:00 [pubmed]
PHST- 2002/02/22 10:01 [medline]
PHST- 2001/12/19 10:00 [entrez]
AID - S0003986101926001 [pii]
AID - 10.1006/abbi.2001.2600 [doi]
PST - ppublish
SO  - Arch Biochem Biophys. 2002 Jan 1;397(1):40-50. doi: 10.1006/abbi.2001.2600.