PMID- 20961592
OWN - NLM
STAT- MEDLINE
DCOM- 20101206
LR  - 20211020
IS  - 1096-0341 (Electronic)
IS  - 0042-6822 (Print)
IS  - 0042-6822 (Linking)
VI  - 408
IP  - 2
DP  - 2010 Dec 20
TI  - Identification of aromatic amino acid residues in conserved region VI of the 
      large polymerase of vesicular stomatitis virus is essential for both guanine-N-7 
      and ribose 2'-O methyltransferases.
PG  - 241-52
LID - 10.1016/j.virol.2010.09.017 [doi]
AB  - Non-segmented negative-sense RNA viruses possess a unique mechanism for mRNA cap 
      methylation. For vesicular stomatitis virus, conserved region VI in the large (L) 
      polymerase protein catalyzes both guanine-N-7 (G-N-7) and ribose 2'-O (2'-O) 
      methyltransferases, and the two methylases share a binding site for the methyl 
      donor S-adenosyl-l-methionine. Unlike conventional mRNA cap methylation, the 2'-O 
      methylation of VSV precedes subsequent G-N-7 methylation. In this study, we found 
      that individual alanine substitutions in two conserved aromatic residues (Y1650 
      and F1691) in region VI of L protein abolished both G-N-7 and 2'-O methylation. 
      However, replacement of one aromatic residue with another aromatic residue did 
      not significantly affect the methyltransferase activities. Our studies provide 
      genetic and biochemical evidence that conserved aromatic residues in region VI of 
      L protein essential for both G-N-7 and 2'-O methylations. In combination with the 
      structural prediction, our results suggest that these aromatic residues may 
      participate in RNA recognition.
CI  - Copyright (c) 2010 Elsevier Inc. All rights reserved.
FAU - Zhang, Xiaodong
AU  - Zhang X
AD  - College of Animal Science, Zhejiang University, Hangzhou, Zhejiang, China.
FAU - Wei, Yongwei
AU  - Wei Y
FAU - Ma, Yuanmei
AU  - Ma Y
FAU - Hu, Songhua
AU  - Hu S
FAU - Li, Jianrong
AU  - Li J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20101018
PL  - United States
TA  - Virology
JT  - Virology
JID - 0110674
RN  - 0 (Amino Acids, Aromatic)
RN  - 0 (RNA Caps)
RN  - 0 (RNA, Viral)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Viral Proteins)
RN  - EC 2.1.1.- (Methyltransferases)
RN  - EC 2.7.7.6 (DNA-Directed RNA Polymerases)
RN  - EC 2.7.7.6 (L polymerase protein, Vesicular stomatitis-Indiana virus)
SB  - IM
MH  - Amino Acid Sequence
MH  - Amino Acid Substitution
MH  - Amino Acids, Aromatic/chemistry
MH  - Animals
MH  - Catalytic Domain/genetics
MH  - Cell Line
MH  - Conserved Sequence
MH  - DNA-Directed RNA Polymerases/*chemistry/genetics/*metabolism
MH  - Methylation
MH  - Methyltransferases/*metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Mutation
MH  - RNA Caps/metabolism
MH  - RNA, Viral/metabolism
MH  - Recombinant Proteins/chemistry/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
MH  - Vesiculovirus/*enzymology/*genetics
MH  - Viral Proteins/*chemistry/genetics/*metabolism
PMC - PMC7111938
EDAT- 2010/10/22 06:00
MHDA- 2010/12/14 06:00
PMCR- 2010/10/18
CRDT- 2010/10/22 06:00
PHST- 2010/07/09 00:00 [received]
PHST- 2010/08/23 00:00 [revised]
PHST- 2010/09/17 00:00 [accepted]
PHST- 2010/10/22 06:00 [entrez]
PHST- 2010/10/22 06:00 [pubmed]
PHST- 2010/12/14 06:00 [medline]
PHST- 2010/10/18 00:00 [pmc-release]
AID - S0042-6822(10)00605-7 [pii]
AID - 10.1016/j.virol.2010.09.017 [doi]
PST - ppublish
SO  - Virology. 2010 Dec 20;408(2):241-52. doi: 10.1016/j.virol.2010.09.017. Epub 2010 
      Oct 18.