PMID- 24634441
OWN - NLM
STAT- MEDLINE
DCOM- 20140715
LR  - 20240321
IS  - 1362-4962 (Electronic)
IS  - 0305-1048 (Print)
IS  - 0305-1048 (Linking)
VI  - 42
IP  - 9
DP  - 2014 May
TI  - SAXS analysis of the tRNA-modifying enzyme complex MnmE/MnmG reveals a novel 
      interaction mode and GTP-induced oligomerization.
PG  - 5978-92
LID - 10.1093/nar/gku213 [doi]
AB  - Transfer ribonucleic acid (tRNA) modifications, especially at the wobble 
      position, are crucial for proper and efficient protein translation. MnmE and MnmG 
      form a protein complex that is implicated in the carboxymethylaminomethyl 
      modification of wobble uridine (cmnm(5)U34) of certain tRNAs. MnmE is a G protein 
      activated by dimerization (GAD), and active guanosine-5'-triphosphate (GTP) 
      hydrolysis is required for the tRNA modification to occur. Although crystal 
      structures of MnmE and MnmG are available, the structure of the MnmE/MnmG complex 
      (MnmEG) and the nature of the nucleotide-induced conformational changes and their 
      relevance for the tRNA modification reaction remain unknown. In this study, we 
      mainly used small-angle X-ray scattering to characterize these conformational 
      changes in solution and to unravel the mode of interaction between MnmE, MnmG and 
      tRNA. In the nucleotide-free state MnmE and MnmG form an unanticipated asymmetric 
      alpha2beta2 complex. Unexpectedly, GTP binding promotes further oligomerization of the 
      MnmEG complex leading to an alpha4beta2 complex. The transition from the alpha2beta2 to the 
      alpha4beta2 complex is fast, reversible and coupled to GTP binding and hydrolysis. We 
      propose a model in which the nucleotide-induced changes in conformation and 
      oligomerization of MnmEG form an integral part of the tRNA modification reaction 
      cycle.
CI  - (c) The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic 
      Acids Research.
FAU - Fislage, Marcus
AU  - Fislage M
AD  - Structural Biology Research Center, VIB, Pleinlaan 2, 1050 Brussel, Belgium 
      Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 
      Brussel, Belgium.
FAU - Brosens, Elke
AU  - Brosens E
AD  - Structural Biology Research Center, VIB, Pleinlaan 2, 1050 Brussel, Belgium 
      Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 
      Brussel, Belgium.
FAU - Deyaert, Egon
AU  - Deyaert E
AD  - Structural Biology Research Center, VIB, Pleinlaan 2, 1050 Brussel, Belgium 
      Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 
      Brussel, Belgium.
FAU - Spilotros, Alessandro
AU  - Spilotros A
AD  - EMBL Hamburg outstation c/o DESY, Notkestrasse 85, Geb. 25A, 22603 Hamburg, 
      Germany.
FAU - Pardon, Els
AU  - Pardon E
AD  - Structural Biology Research Center, VIB, Pleinlaan 2, 1050 Brussel, Belgium 
      Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 
      Brussel, Belgium.
FAU - Loris, Remy
AU  - Loris R
AD  - Structural Biology Research Center, VIB, Pleinlaan 2, 1050 Brussel, Belgium 
      Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 
      Brussel, Belgium.
FAU - Steyaert, Jan
AU  - Steyaert J
AD  - Structural Biology Research Center, VIB, Pleinlaan 2, 1050 Brussel, Belgium 
      Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 
      Brussel, Belgium.
FAU - Garcia-Pino, Abel
AU  - Garcia-Pino A
AD  - Structural Biology Research Center, VIB, Pleinlaan 2, 1050 Brussel, Belgium 
      Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 
      Brussel, Belgium.
FAU - Versees, Wim
AU  - Versees W
AD  - Structural Biology Research Center, VIB, Pleinlaan 2, 1050 Brussel, Belgium 
      Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 
      Brussel, Belgium Wim.Versees@vib-vub.be.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140314
PL  - England
TA  - Nucleic Acids Res
JT  - Nucleic acids research
JID - 0411011
RN  - 0 (Escherichia coli Proteins)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - 9014-25-9 (RNA, Transfer)
RN  - EC 2.1.- (MnmG protein, E coli)
RN  - EC 2.1.- (One-Carbon Group Transferases)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - EC 3.6.1.- (MnmE protein, E coli)
SB  - IM
MH  - Catalytic Domain
MH  - Escherichia coli/*enzymology
MH  - Escherichia coli Proteins/*chemistry
MH  - GTP Phosphohydrolases/*chemistry
MH  - Guanosine Triphosphate/*chemistry
MH  - Hydrolysis
MH  - Kinetics
MH  - Molecular Docking Simulation
MH  - One-Carbon Group Transferases/*chemistry
MH  - Protein Binding
MH  - Protein Multimerization
MH  - Protein Structure, Quaternary
MH  - Protein Structure, Secondary
MH  - RNA, Transfer/chemistry
MH  - Scattering, Small Angle
MH  - X-Ray Diffraction
PMC - PMC4027165
EDAT- 2014/03/19 06:00
MHDA- 2014/07/16 06:00
PMCR- 2014/03/14
CRDT- 2014/03/18 06:00
PHST- 2014/03/18 06:00 [entrez]
PHST- 2014/03/19 06:00 [pubmed]
PHST- 2014/07/16 06:00 [medline]
PHST- 2014/03/14 00:00 [pmc-release]
AID - gku213 [pii]
AID - 10.1093/nar/gku213 [doi]
PST - ppublish
SO  - Nucleic Acids Res. 2014 May;42(9):5978-92. doi: 10.1093/nar/gku213. Epub 2014 Mar 
      14.