PMID- 28208632
OWN - NLM
STAT- MEDLINE
DCOM- 20171108
LR  - 20201209
IS  - 2218-273X (Electronic)
IS  - 2218-273X (Linking)
VI  - 7
IP  - 1
DP  - 2017 Feb 10
TI  - Cross-Talk between Dnmt2-Dependent tRNA Methylation and Queuosine Modification.
LID - 10.3390/biom7010014 [doi]
LID - 14
AB  - Enzymes of the Dnmt2 family of methyltransferases have yielded a number of 
      unexpected discoveries. The first surprise came more than ten years ago when it 
      was realized that, rather than being DNA methyltransferases, Dnmt2 enzymes 
      actually are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, 
      foremost C38 (m5C38) of tRNAAsp. The second unanticipated finding was our recent 
      discovery of a nutritional regulation of Dnmt2 in the fission yeast 
      Schizosaccharomyces pombe. Significantly, the presence of the nucleotide 
      queuosine in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro 
      in S. pombe. Queuine, the respective base, is a hypermodified guanine analog that 
      is synthesized from guanosine-5'-triphosphate (GTP) by bacteria. Interestingly, 
      most eukaryotes have queuosine in their tRNA. However, they cannot synthesize it 
      themselves, but rather salvage it from food or from gut microbes. The queuine 
      obtained from these sources comes from the breakdown of tRNAs, where the queuine 
      ultimately was synthesized by bacteria. Queuine thus has been termed a 
      micronutrient. This review summarizes the current knowledge of Dnmt2 methylation 
      and queuosine modification with respect to translation as well as the organismal 
      consequences of the absence of these modifications. Models for the functional 
      cooperation between these modifications and its wider implications are discussed.
FAU - Ehrenhofer-Murray, Ann E
AU  - Ehrenhofer-Murray AE
AD  - Institut fur Biologie, Humboldt-Universitat zu Berlin, 10099 Berlin, Germany. 
      ann.ehrenhofer-murray@hu-berlin.de.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20170210
PL  - Switzerland
TA  - Biomolecules
JT  - Biomolecules
JID - 101596414
RN  - 57072-36-3 (Nucleoside Q)
RN  - 9014-25-9 (RNA, Transfer)
RN  - EC 2.1.1.37 (DNA (Cytosine-5-)-Methyltransferases)
SB  - IM
MH  - Animals
MH  - Bacteria/genetics/metabolism
MH  - DNA (Cytosine-5-)-Methyltransferases/*metabolism
MH  - Gene Expression Regulation, Fungal
MH  - Humans
MH  - Methylation
MH  - Nucleoside Q/*chemistry/metabolism
MH  - RNA, Transfer/*chemistry
MH  - Schizosaccharomyces/genetics/metabolism
PMC - PMC5372726
OTO - NOTNLM
OT  - Dnmt2
OT  - Pmt1
OT  - anticodon modification
OT  - epitranscriptomics
OT  - queuine
OT  - queuosine
OT  - tRNA cleavage
OT  - translation
COIS- The author declares no conflict of interest.
EDAT- 2017/02/18 06:00
MHDA- 2017/11/09 06:00
PMCR- 2017/03/01
CRDT- 2017/02/18 06:00
PHST- 2016/12/19 00:00 [received]
PHST- 2017/02/02 00:00 [revised]
PHST- 2017/02/02 00:00 [accepted]
PHST- 2017/02/18 06:00 [entrez]
PHST- 2017/02/18 06:00 [pubmed]
PHST- 2017/11/09 06:00 [medline]
PHST- 2017/03/01 00:00 [pmc-release]
AID - biom7010014 [pii]
AID - biomolecules-07-00014 [pii]
AID - 10.3390/biom7010014 [doi]
PST - epublish
SO  - Biomolecules. 2017 Feb 10;7(1):14. doi: 10.3390/biom7010014.