PMID- 20932061
OWN - NLM
STAT- MEDLINE
DCOM- 20101222
LR  - 20231213
IS  - 1520-4995 (Electronic)
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 49
IP  - 45
DP  - 2010 Nov 16
TI  - The C-terminus of nucleolin promotes the formation of the c-MYC G-quadruplex and 
      inhibits c-MYC promoter activity.
PG  - 9706-14
LID - 10.1021/bi100509s [doi]
AB  - Nucleolin, the most abundant nucleolar phosphoprotein of eukaryotic cells, is 
      known primarily for its role in ribosome biogenesis and cell proliferation. It 
      is, however, a multifunctional protein that, depending on the cellular context, 
      can drive either cell proliferation or apoptosis. Our laboratory recently 
      demonstrated that nucleolin can function as a repressor of c-MYC transcription by 
      binding to and stabilizing the formation of a G-quadruplex structure in a region 
      of the c-MYC promoter responsible for controlling 85-90% of c-MYC's 
      transcriptional activity. In this study, we investigate the structural elements 
      of nucleolin that are required for c-MYC repression. The effect of nucleolin 
      deletion mutants on the formation and stability of the c-MYC G-quadruplex, as 
      well as c-MYC transcriptional activity, was assessed by circular dichroism 
      spectropolarimetry, thermal stability, and in vitro transcription. Here we report 
      that nucleolin's RNA binding domains 3 and 4, as well as the 
      arginine-glycine-glycine (RGG) domain, are required to repress c-MYC 
      transcription.
FAU - Gonzalez, Veronica
AU  - Gonzalez V
AD  - College of Pharmacy, Department of Pharmacology and Toxicology, University of 
      Arizona, Tucson, Arizona 85721, United States.
FAU - Hurley, Laurence H
AU  - Hurley LH
LA  - eng
GR  - R01 GM085585-02/GM/NIGMS NIH HHS/United States
GR  - P50 CA095060-090004/CA/NCI NIH HHS/United States
GR  - CA95060/CA/NCI NIH HHS/United States
GR  - R01 CA094166-05S2/CA/NCI NIH HHS/United States
GR  - CA94166/CA/NCI NIH HHS/United States
GR  - P50 CA095060/CA/NCI NIH HHS/United States
GR  - R01 CA094166-05S1/CA/NCI NIH HHS/United States
GR  - GM085585/GM/NIGMS NIH HHS/United States
GR  - R01 GM085585-01/GM/NIGMS NIH HHS/United States
GR  - R01 CA094166/CA/NCI NIH HHS/United States
GR  - R01 GM085585/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20101021
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (DNA Primers)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Proto-Oncogene Proteins c-myc)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Recombinant Proteins)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Cell Division
MH  - DNA Primers
MH  - Gene Deletion
MH  - *Genes, myc
MH  - Genetic Vectors
MH  - Kinetics
MH  - Mammals
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Nuclear Proteins/*genetics/metabolism
MH  - Phosphoproteins/*genetics/metabolism
MH  - *Promoter Regions, Genetic
MH  - Proto-Oncogene Proteins c-myc/*genetics/metabolism
MH  - RNA-Binding Proteins/*genetics/metabolism
MH  - Recombinant Proteins/isolation & purification/metabolism
MH  - Ribosomes
MH  - *Sequence Deletion
MH  - *Transcription, Genetic
MH  - Nucleolin
PMC - PMC2976822
MID - NIHMS245680
EDAT- 2010/10/12 06:00
MHDA- 2010/12/24 06:00
PMCR- 2011/11/16
CRDT- 2010/10/12 06:00
PHST- 2010/10/12 06:00 [entrez]
PHST- 2010/10/12 06:00 [pubmed]
PHST- 2010/12/24 06:00 [medline]
PHST- 2011/11/16 00:00 [pmc-release]
AID - 10.1021/bi100509s [doi]
PST - ppublish
SO  - Biochemistry. 2010 Nov 16;49(45):9706-14. doi: 10.1021/bi100509s. Epub 2010 Oct 
      21.