PMID- 11438540
OWN - NLM
STAT- MEDLINE
DCOM- 20011018
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 276
IP  - 35
DP  - 2001 Aug 31
TI  - Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation 
      factor 2 kinase double-stranded RNA-activated protein kinase.
PG  - 32522-30
AB  - Nuclear factor 90 (NF90) is a member of an expanding family of double-stranded 
      (ds) RNA-binding proteins thought to be involved in gene expression. Originally 
      identified in complex with nuclear factor 45 (NF45) as a sequence-specific 
      DNA-binding protein, NF90 contains two double stranded RNA-binding motifs 
      (dsRBMs) and interacts with highly structured RNAs as well as the dsRNA-activated 
      protein kinase, PKR. In this report, we characterize the biochemical interactions 
      between these two dsRBM containing proteins. NF90 binds to PKR through two 
      independent mechanisms: an RNA-independent interaction occurs between the N 
      terminus of NF90 and the C-terminal region of PKR, and an RNA-dependent 
      interaction is mediated by the dsRBMs of the two proteins. Co-immunoprecipitation 
      analysis demonstrates that NF90, NF45, and PKR form a complex in both nuclear and 
      cytosolic extracts, and both proteins serve as substrates for PKR in vitro. NF90 
      is phosphorylated by PKR in its RNA-binding domain, and this reaction is 
      partially blocked by the NF90 N-terminal region. The C-terminal region also 
      inhibits PKR function, probably through competitive binding to dsRNA. A model for 
      NF90-PKR interactions is proposed.
FAU - Parker, L M
AU  - Parker LM
AD  - Department of Biochemistry and Molecular Biology, New Jersey Medical School, 
      University of Medicine and Dentistry, New Jersey, Newark, New Jersey 07103-2714, 
      USA.
FAU - Fierro-Monti, I
AU  - Fierro-Monti I
FAU - Mathews, M B
AU  - Mathews MB
LA  - eng
GR  - AI34552/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20010703
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (ILF2 protein, human)
RN  - 0 (NFATC Transcription Factors)
RN  - 0 (Nuclear Factor 45 Protein)
RN  - 0 (Nuclear Factor 90 Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (RNA, Double-Stranded)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Transcription Factors)
RN  - 63231-63-0 (RNA)
RN  - EC 2.7.11.1 (eIF-2 Kinase)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Cell Nucleus/metabolism
MH  - Cytosol/metabolism
MH  - DNA-Binding Proteins/chemistry/genetics/*metabolism
MH  - Kinetics
MH  - Models, Molecular
MH  - NFATC Transcription Factors
MH  - Nuclear Factor 45 Protein
MH  - Nuclear Factor 90 Proteins
MH  - Nuclear Proteins/metabolism
MH  - Nucleic Acid Conformation
MH  - Protein Conformation
MH  - RNA/chemistry/metabolism
MH  - RNA, Double-Stranded/chemistry/metabolism
MH  - RNA-Binding Proteins/chemistry/metabolism
MH  - Recombinant Fusion Proteins/chemistry/metabolism
MH  - Sequence Deletion
MH  - Substrate Specificity
MH  - Transcription Factors/chemistry/genetics/*metabolism
MH  - eIF-2 Kinase/chemistry/*metabolism
EDAT- 2001/07/05 10:00
MHDA- 2001/10/19 10:01
CRDT- 2001/07/05 10:00
PHST- 2001/07/05 10:00 [pubmed]
PHST- 2001/10/19 10:01 [medline]
PHST- 2001/07/05 10:00 [entrez]
AID - S0021-9258(20)77770-7 [pii]
AID - 10.1074/jbc.M104408200 [doi]
PST - ppublish
SO  - J Biol Chem. 2001 Aug 31;276(35):32522-30. doi: 10.1074/jbc.M104408200. Epub 2001 
      Jul 3.