PMID- 18955487
OWN - NLM
STAT- MEDLINE
DCOM- 20090313
LR  - 20210206
IS  - 0021-9258 (Print)
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Linking)
VI  - 283
IP  - 52
DP  - 2008 Dec 26
TI  - The CP2 domain of leucyl-tRNA synthetase is crucial for amino acid activation and 
      post-transfer editing.
PG  - 36608-16
LID - 10.1074/jbc.M806745200 [doi]
AB  - Leucyl-tRNA synthetase (LeuRS) has an insertion domain, called connective peptide 
      2 (CP2), either directly preceding or following the editing domain (CP1 domain), 
      depending on the species. The global structures of the CP2 domains from all 
      LeuRSs are similar. Although the CP1 domain has been extensively explored to be 
      responsible for hydrolysis of mischarged tRNALeu, the role of the CP2 domain 
      remains undefined. In the present work, deletion of the CP2 domain of Giardia 
      lamblia LeuRS (GlLeuRS) showed that the CP2 domain is indispensable for amino 
      acid activation and post-transfer editing and that it contributes to 
      LeuRS-tRNALeu binding affinity. In addition, its functions are conserved in both 
      eukaryotic/archaeal and prokaryotic LeuRSs from G. lamblia, Pyrococcus horikoshii 
      (PhLeuRS), and Escherichia coli (EcLeuRS). Alanine scanning and site-directed 
      mutagenesis assays of the CP2 domain identified several residues that are crucial 
      for its various functions. Data from the chimeric mutants, which replaced the CP2 
      domain of GlLeuRS with either PhLeuRS or EcLeuRS, showed that the CP2 domain of 
      PhLeuRS but not that of EcLeuRS can partially restore amino acid activation and 
      post-transfer editing functions, suggesting that the functions of the CP2 domain 
      are dependent on its location in the primary sequence of LeuRS.
FAU - Zhou, Xiao-Long
AU  - Zhou XL
AD  - State Key Laboratory of Molecular Biology and Graduate School of the Chinese 
      Academy of Sciences, Institute of Biochemistry and Cell Biology, The Chinese 
      Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China.
FAU - Zhu, Bin
AU  - Zhu B
FAU - Wang, En-Duo
AU  - Wang ED
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20081027
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 9014-25-9 (RNA, Transfer)
RN  - EC 6.1.1.4 (Leucine-tRNA Ligase)
RN  - GMW67QNF9C (Leucine)
RN  - OF5P57N2ZX (Alanine)
SB  - IM
MH  - Alanine/chemistry
MH  - Amino Acid Sequence
MH  - Animals
MH  - Escherichia coli/*metabolism
MH  - Giardia lamblia/*metabolism
MH  - Hydrolysis
MH  - Leucine/chemistry
MH  - Leucine-tRNA Ligase/*chemistry/metabolism
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Protein Structure, Tertiary
MH  - Pyrococcus horikoshii/*metabolism
MH  - *RNA Editing
MH  - RNA, Transfer/*chemistry
MH  - Sequence Homology, Amino Acid
PMC - PMC2662312
EDAT- 2008/10/29 09:00
MHDA- 2009/03/14 09:00
PMCR- 2009/12/26
CRDT- 2008/10/29 09:00
PHST- 2008/10/29 09:00 [pubmed]
PHST- 2009/03/14 09:00 [medline]
PHST- 2008/10/29 09:00 [entrez]
PHST- 2009/12/26 00:00 [pmc-release]
AID - S0021-9258(20)49670-X [pii]
AID - 36608 [pii]
AID - 10.1074/jbc.M806745200 [doi]
PST - ppublish
SO  - J Biol Chem. 2008 Dec 26;283(52):36608-16. doi: 10.1074/jbc.M806745200. Epub 2008 
      Oct 27.