PMID- 25149208
OWN - NLM
STAT- MEDLINE
DCOM- 20150113
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1839
IP  - 11
DP  - 2014 Nov
TI  - Role of the OB-fold of RNA helicase A in the synthesis of HIV-1 RNA.
PG  - 1069-78
LID - S1874-9399(14)00226-0 [pii]
LID - 10.1016/j.bbagrm.2014.08.008 [doi]
AB  - RNA helicase A (RHA), a DExD/H protein, contains a stretch of repeated arginine 
      and glycine-glycine (RGG) residues and an oligonucleotide/oligosaccharide-binding 
      fold (OB-fold) at the C-terminus. RHA has been reported to function as a 
      transcriptional cofactor. This study shows the role of RGG and OB-fold domains of 
      RHA in the activation of transcription and splicing of HIV-1 RNA. RHA stimulates 
      HIV-1 transcription by enhancing the occupancy of RNA polymerase II on the 
      proviral DNA. Deletion of RGG or both RGG and OB-fold does not change the 
      transcriptional activity of RHA, nor does the stability of viral RNA. However, 
      deletion of both RGG and OB-fold rather than deletion of RGG only results in less 
      production of multiply spliced 6D RNAs. The results suggest that the OB-fold is 
      involved in modulating HIV-1 RNA splicing in the context of some HIV-1 strains 
      while it is dispensable for the activation of HIV-1 transcription.
CI  - Copyright (c) 2014 Elsevier B.V. All rights reserved.
FAU - Xing, Li
AU  - Xing L
AD  - Lady Davis Institute for Medical Research and McGill AIDS Centre, Jewish General 
      Hospital, Montreal, Quebec, Canada; Department of Medicine, McGill University, 
      Montreal, Quebec, Canada. Electronic address: xingli107@gmail.com.
FAU - Niu, Meijuan
AU  - Niu M
AD  - Lady Davis Institute for Medical Research and McGill AIDS Centre, Jewish General 
      Hospital, Montreal, Quebec, Canada; Department of Medicine, McGill University, 
      Montreal, Quebec, Canada.
FAU - Kleiman, Lawrence
AU  - Kleiman L
AD  - Lady Davis Institute for Medical Research and McGill AIDS Centre, Jewish General 
      Hospital, Montreal, Quebec, Canada; Department of Medicine, McGill University, 
      Montreal, Quebec, Canada. Electronic address: lawrence.kleiman@mcgill.ca.
LA  - eng
GR  - Canadian Institutes of Health Research/Canada
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140819
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Oligonucleotides)
RN  - 0 (Oligosaccharides)
RN  - 0 (RNA, Viral)
RN  - EC 3.6.1.- (DHX9 protein, human)
RN  - EC 3.6.4.13 (DEAD-box RNA Helicases)
SB  - IM
MH  - Binding Sites
MH  - DEAD-box RNA Helicases/*chemistry/*metabolism
MH  - Gene Expression Regulation, Viral
MH  - HEK293 Cells
MH  - HIV-1/*genetics
MH  - Humans
MH  - Neoplasm Proteins/*chemistry/*metabolism
MH  - Oligonucleotides/*metabolism
MH  - Oligosaccharides/*metabolism
MH  - Protein Folding
MH  - Protein Structure, Tertiary/physiology
MH  - RNA Splicing
MH  - RNA, Viral/*biosynthesis
OTO - NOTNLM
OT  - HIV-1
OT  - OB-fold
OT  - RNA helicase A
OT  - Splicing
OT  - Transcription
EDAT- 2014/08/26 06:00
MHDA- 2015/01/15 06:00
CRDT- 2014/08/24 06:00
PHST- 2014/03/23 00:00 [received]
PHST- 2014/07/25 00:00 [revised]
PHST- 2014/08/12 00:00 [accepted]
PHST- 2014/08/24 06:00 [entrez]
PHST- 2014/08/26 06:00 [pubmed]
PHST- 2015/01/15 06:00 [medline]
AID - S1874-9399(14)00226-0 [pii]
AID - 10.1016/j.bbagrm.2014.08.008 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2014 Nov;1839(11):1069-78. doi: 
      10.1016/j.bbagrm.2014.08.008. Epub 2014 Aug 19.