PMID- 18029576
OWN - NLM
STAT- MEDLINE
DCOM- 20080428
LR  - 20120802
IS  - 1746-8272 (Electronic)
IS  - 0261-3166 (Linking)
IP  - 51
DP  - 2007
TI  - Aminoacyl-tRNA surveillance by EF-Tu in mammalian mitochondria.
PG  - 41-2
AB  - Aminoacyl-tRNA synthetases specifically recognize their cognate tRNAs and ensure 
      the accuracy of translation. However, in mammalian mitochondria, seryl-tRNA 
      synthetase (mt SerRS) significantly misacylates tRNA(Gln), indicating the 
      presence of another mechanism to be required to maintain the fidelity of 
      mitochondrial protein synthesis. We have revealed that mammalian mitochondrial 
      elongation factor Tu (mt EF-Tu) tends to interact with seryl-tRNA(Gln) with lower 
      affinity than glutaminyl-tRNA(Gln) and seryl-tRNA(Ser). This result proposes that 
      mt EF-Tu has a critical role to maintain the translational fidelity by 
      surveillance of aminoacyl-tRNAs for quality control.
FAU - Nagao, Asuteka
AU  - Nagao A
AD  - Department of Chemistry and Biotechnology, School of Engineering, The University 
      of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
FAU - Suzuki, Takeo
AU  - Suzuki T
FAU - Suzuki, Tsutomu
AU  - Suzuki T
LA  - eng
PT  - Journal Article
PL  - England
TA  - Nucleic Acids Symp Ser (Oxf)
JT  - Nucleic acids symposium series (2004)
JID - 101259965
RN  - 0 (Mitochondrial Proteins)
RN  - 0 (RNA, Transfer, Amino Acyl)
RN  - EC 3.6.1.- (Peptide Elongation Factor Tu)
SB  - IM
MH  - Animals
MH  - Cattle
MH  - Mitochondria/enzymology/*genetics
MH  - Mitochondrial Proteins/*biosynthesis
MH  - Peptide Elongation Factor Tu/*physiology
MH  - RNA, Transfer, Amino Acyl/*metabolism
MH  - *Transfer RNA Aminoacylation
EDAT- 2007/11/22 09:00
MHDA- 2008/04/29 09:00
CRDT- 2007/11/22 09:00
PHST- 2007/11/22 09:00 [pubmed]
PHST- 2008/04/29 09:00 [medline]
PHST- 2007/11/22 09:00 [entrez]
AID - 51/1/41 [pii]
AID - 10.1093/nass/nrm021 [doi]
PST - ppublish
SO  - Nucleic Acids Symp Ser (Oxf). 2007;(51):41-2. doi: 10.1093/nass/nrm021.