PMID- 24794712
OWN - NLM
STAT- MEDLINE
DCOM- 20150810
LR  - 20140603
IS  - 1520-6882 (Electronic)
IS  - 0003-2700 (Linking)
VI  - 86
IP  - 11
DP  - 2014 Jun 3
TI  - In situ monitoring of structural changes during formation of 30S translation 
      initiation complex by energy dissipation measurement using 27-MHz quartz-crystal 
      microbalance.
PG  - 5406-15
LID - 10.1021/ac500487b [doi]
AB  - Ribosome is a bionanomachine that facilitates an orderly translation process 
      during protein synthesis in living cells. Real-time monitoring of conformational 
      changes in ribosomal subunits in aqueous solution is important to understand the 
      regulatory mechanism of protein synthesis, because conformational changes in 
      ribosome in E. coli have been predicted to operate the switch from translation 
      initiation to an elongation process during translation. We performed an energy 
      dissipation measurement by using a quartz-crystal microbalance-admittance (QCM-A) 
      technique for in situ monitoring of conformational changes in pre-30S translation 
      initiation complex in response to the binding of fMet-tRNA(fMet) in aqueous 
      solution. The addition of fMet-tRNA(fMet) caused changes in the physical property 
      (increased dehydration and elasticity) in 30S ribosomal subunit in the presence 
      of mRNA and IF2/guanosine 5'-triphosphate (GTP) on the QCM plate. Furthermore, 
      two sequential changes triggered by the addition of fMet-tRNA(fMet) were observed 
      in 30S ribosomal subunit bound to mRNA in the presence of IF2/GTP and IF3. These 
      observations suggest that the structural changes in 30S ribosomal subunit caused 
      by the binding of fMet-tRNA(fMet) with IF2/GTP in the presence of IF3 could act 
      as a switch to regulate the orderly processing in the construction of translation 
      initiation complex, because the structural distinction can be a guidepost in the 
      process for the relevant biomolecules.
FAU - Furusawa, Hiroyuki
AU  - Furusawa H
AD  - Innovative Flex Course for Frontier Organic Material Systems (iFront), Yamagata 
      University , 4-3-16 Jonan, Yonezawa, Yamagata 992-8510, Japan.
FAU - Tsuyuki, Yumi
AU  - Tsuyuki Y
FAU - Takahashi, Shuntaro
AU  - Takahashi S
FAU - Okahata, Yoshio
AU  - Okahata Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140512
PL  - United States
TA  - Anal Chem
JT  - Analytical chemistry
JID - 0370536
RN  - 0 (Eukaryotic Initiation Factor-2)
RN  - 0 (Eukaryotic Initiation Factor-3)
RN  - 0 (Immobilized Nucleic Acids)
RN  - 0 (RNA, Transfer, Met)
RN  - 86-01-1 (Guanosine Triphosphate)
SB  - IM
MH  - Biotinylation
MH  - Cell-Free System
MH  - Escherichia coli/chemistry
MH  - Eukaryotic Initiation Factor-2/chemistry
MH  - Eukaryotic Initiation Factor-3/chemistry
MH  - Guanosine Triphosphate/chemistry
MH  - Immobilized Nucleic Acids
MH  - Nucleic Acid Conformation
MH  - RNA, Transfer, Met/chemistry
MH  - Ribosome Subunits, Small, Bacterial/*chemistry
MH  - Ribosomes/*chemistry
EDAT- 2014/05/06 06:00
MHDA- 2015/08/11 06:00
CRDT- 2014/05/06 06:00
PHST- 2014/05/06 06:00 [entrez]
PHST- 2014/05/06 06:00 [pubmed]
PHST- 2015/08/11 06:00 [medline]
AID - 10.1021/ac500487b [doi]
PST - ppublish
SO  - Anal Chem. 2014 Jun 3;86(11):5406-15. doi: 10.1021/ac500487b. Epub 2014 May 12.