PMID- 27051866
OWN - NLM
STAT- MEDLINE
DCOM- 20170504
LR  - 20181113
IS  - 2375-2548 (Electronic)
IS  - 2375-2548 (Linking)
VI  - 2
IP  - 3
DP  - 2016 Mar
TI  - Template-dependent nucleotide addition in the reverse (3'-5') direction by 
      Thg1-like protein.
PG  - e1501397
LID - 10.1126/sciadv.1501397 [doi]
LID - e1501397
AB  - Thg1-like protein (TLP) catalyzes the addition of a nucleotide to the 5'-end of 
      truncated transfer RNA (tRNA) species in a Watson-Crick template-dependent 
      manner. The reaction proceeds in two steps: the activation of the 5'-end by 
      adenosine 5'-triphosphate (ATP)/guanosine 5'-triphosphate (GTP), followed by 
      nucleotide addition. Structural analyses of the TLP and its reaction 
      intermediates have revealed the atomic detail of the template-dependent 
      elongation reaction in the 3'-5' direction. The enzyme creates two substrate 
      binding sites for the first- and second-step reactions in the vicinity of one 
      reaction center consisting of two Mg(2+) ions, and the two reactions are executed 
      at the same reaction center in a stepwise fashion. When the incoming nucleotide 
      is bound to the second binding site with Watson-Crick hydrogen bonds, the 3'-OH 
      of the incoming nucleotide and the 5'-triphosphate of the tRNA are moved to the 
      reaction center where the first reaction has occurred. That the 3'-5' elongation 
      enzyme performs this elaborate two-step reaction in one catalytic center suggests 
      that these two reactions have been inseparable throughout the process of protein 
      evolution. Although TLP and Thg1 have similar tetrameric organization, the tRNA 
      binding mode of TLP is different from that of Thg1, a tRNA(His)-specific G-1 
      addition enzyme. Each tRNA(His) binds to three of the four Thg1 tetramer 
      subunits, whereas in TLP, tRNA only binds to a dimer interface and the elongation 
      reaction is terminated by measuring the accepter stem length through the flexible 
      beta-hairpin. Furthermore, mutational analyses show that tRNA(His) is bound to TLP 
      in a similar manner as Thg1, thus indicating that TLP has a dual binding mode.
FAU - Kimura, Shoko
AU  - Kimura S
AD  - Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan.
FAU - Suzuki, Tateki
AU  - Suzuki T
AD  - Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan.
FAU - Chen, Meirong
AU  - Chen M
AD  - Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan.
FAU - Kato, Koji
AU  - Kato K
AUID- ORCID: 0000-0001-9846-5903
AD  - Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan.; 
      Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan.
FAU - Yu, Jian
AU  - Yu J
AD  - Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan.
FAU - Nakamura, Akiyoshi
AU  - Nakamura A
AD  - Bioproduction Research Institute, National Institute of Advanced Industrial 
      Science and Technology (AIST), Sapporo 062-8517, Japan.
FAU - Tanaka, Isao
AU  - Tanaka I
AD  - Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan.
FAU - Yao, Min
AU  - Yao M
AUID- ORCID: 0000-0003-1687-5904
AD  - Graduate School of Life Science, Hokkaido University, Sapporo 060-0810, Japan.; 
      Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20160325
PL  - United States
TA  - Sci Adv
JT  - Science advances
JID - 101653440
RN  - 0 (Anticodon)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - 9014-25-9 (RNA, Transfer)
RN  - EC 2.7.7.- (Nucleotidyltransferases)
SB  - IM
MH  - Adenosine Triphosphate/metabolism
MH  - Anticodon
MH  - Catalysis
MH  - Guanosine Triphosphate/metabolism
MH  - Methanosarcina/enzymology
MH  - Models, Biological
MH  - Models, Molecular
MH  - Mutation
MH  - Nucleic Acid Conformation
MH  - Nucleotidyltransferases/chemistry/*metabolism
MH  - Protein Binding
MH  - Protein Conformation
MH  - RNA, Transfer/chemistry/genetics/*metabolism
PMC - PMC4820378
OTO - NOTNLM
OT  - 3'-5' addition
OT  - TLP
OT  - biomolecules
OT  - crystal structure
OT  - nucleotides
OT  - reverse polymerization
OT  - tRNA
EDAT- 2016/04/07 06:00
MHDA- 2017/05/05 06:00
PMCR- 2016/03/25
CRDT- 2016/04/07 06:00
PHST- 2015/10/07 00:00 [received]
PHST- 2016/02/04 00:00 [accepted]
PHST- 2016/04/07 06:00 [entrez]
PHST- 2016/04/07 06:00 [pubmed]
PHST- 2017/05/05 06:00 [medline]
PHST- 2016/03/25 00:00 [pmc-release]
AID - 1501397 [pii]
AID - 10.1126/sciadv.1501397 [doi]
PST - epublish
SO  - Sci Adv. 2016 Mar 25;2(3):e1501397. doi: 10.1126/sciadv.1501397. eCollection 2016 
      Mar.