PMID- 34302476
OWN - NLM
STAT- MEDLINE
DCOM- 20211007
LR  - 20211007
IS  - 1362-4962 (Electronic)
IS  - 0305-1048 (Print)
IS  - 0305-1048 (Linking)
VI  - 49
IP  - 14
DP  - 2021 Aug 20
TI  - The RGG domain in the C-terminus of the DEAD box helicases Dbp2 and Ded1 is 
      necessary for G-quadruplex destabilization.
PG  - 8339-8354
LID - 10.1093/nar/gkab620 [doi]
AB  - The identification of G-quadruplex (G4) binding proteins and insights into their 
      mechanism of action are important for understanding the regulatory functions of 
      G4 structures. Here, we performed an unbiased affinity-purification assay coupled 
      with mass spectrometry and identified 30 putative G4 binding proteins from the 
      fission yeast Schizosaccharomyces pombe. Gene ontology analysis of the molecular 
      functions enriched in this pull-down assay included mRNA binding, RNA helicase 
      activity, and translation regulator activity. We focused this study on three of 
      the identified proteins that possessed putative arginine-glycine-glycine (RGG) 
      domains, namely the Stm1 homolog Oga1 and the DEAD box RNA helicases Dbp2 and 
      Ded1. We found that Oga1, Dbp2, and Ded1 bound to both DNA and RNA G4s in vitro. 
      Both Dbp2 and Ded1 bound to G4 structures through the RGG domain located in the 
      C-terminal region of the helicases, and point mutations in this domain weakened 
      the G4 binding properties of the helicases. Dbp2 and Ded1 destabilized less 
      thermostable G4 RNA and DNA structures, and this ability was independent of ATP 
      but dependent on the RGG domain. Our study provides the first evidence that the 
      RGG motifs in DEAD box helicases are necessary for both G4 binding and G4 
      destabilization.
CI  - (c) The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic 
      Acids Research.
FAU - Yan, Kevin Kok-Phen
AU  - Yan KK
AD  - Department of Medical Biochemistry and Biophysics, Umea University, 901 87 Umea, 
      Sweden.
FAU - Obi, Ikenna
AU  - Obi I
AD  - Department of Medical Biochemistry and Biophysics, Umea University, 901 87 Umea, 
      Sweden.
FAU - Sabouri, Nasim
AU  - Sabouri N
AUID- ORCID: 0000-0002-4541-7702
AD  - Department of Medical Biochemistry and Biophysics, Umea University, 901 87 Umea, 
      Sweden.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Nucleic Acids Res
JT  - Nucleic acids research
JID - 0411011
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Oga1 protein, S pombe)
RN  - 0 (Schizosaccharomyces pombe Proteins)
RN  - 0 (Stm1 protein, S pombe)
RN  - EC 2.7.7.- (DHX16 protein, human)
RN  - EC 2.7.7.-. (sum3 protein, S pombe)
RN  - EC 3.6.4.13 (DEAD-box RNA Helicases)
RN  - EC 3.6.4.13 (RNA Helicases)
SB  - IM
MH  - Cell Cycle Proteins/*genetics
MH  - DEAD-box RNA Helicases/*genetics
MH  - DNA-Binding Proteins/*genetics
MH  - *G-Quadruplexes
MH  - Humans
MH  - Membrane Proteins/*genetics
MH  - Protein Binding/genetics
MH  - Protein Domains/genetics
MH  - RNA Helicases/*genetics
MH  - Schizosaccharomyces/genetics
MH  - Schizosaccharomyces pombe Proteins/*genetics
PMC - PMC8373067
EDAT- 2021/07/25 06:00
MHDA- 2021/10/08 06:00
PMCR- 2021/07/24
CRDT- 2021/07/24 12:05
PHST- 2021/07/07 00:00 [accepted]
PHST- 2021/07/02 00:00 [revised]
PHST- 2020/10/31 00:00 [received]
PHST- 2021/07/25 06:00 [pubmed]
PHST- 2021/10/08 06:00 [medline]
PHST- 2021/07/24 12:05 [entrez]
PHST- 2021/07/24 00:00 [pmc-release]
AID - 6327677 [pii]
AID - gkab620 [pii]
AID - 10.1093/nar/gkab620 [doi]
PST - ppublish
SO  - Nucleic Acids Res. 2021 Aug 20;49(14):8339-8354. doi: 10.1093/nar/gkab620.