Cellular nucleic acid binding protein binds G-rich single-stranded nucleic acids and may function as a nucleic acid chaperone

2008 ◽  
Vol 103 (3) ◽  
pp. 1013-1036 ◽  
Author(s):  
Pablo Armas ◽  
Sofía Nasif ◽  
Nora B. Calcaterra
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Binding Protein ◽  
Nucleic Acid Binding ◽  
Nucleic Acid Binding Protein ◽  
Acid Binding Protein ◽  
Nucleic Acid Chaperone

scholarly journals NABP1, a novel RORγ-regulated gene encoding a single-stranded nucleic-acid-binding protein

2006 ◽  
Vol 397 (1) ◽  
pp. 89-99 ◽  
Author(s):  
Hong Soon Kang ◽  
Ju Youn Beak ◽  
Yong-Sik Kim ◽  
Robert M. Petrovich ◽  
Jennifer B. Collins ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Binding Protein ◽  
Size Exclusion ◽  
Binding Motif ◽  
Nucleic Acid Binding ◽  
Wild Type ◽  
Gene Encoding ◽  
Nucleic Acid Binding Protein ◽  
Acid Binding Protein

RORγ2 (retinoid-related orphan receptor γ2) plays a critical role in the regulation of thymopoiesis. Microarray analysis was performed in order to uncover differences in gene expression between thymocytes of wild-type and RORγ−/− mice. This analysis identified a novel gene encoding a 22 kDa protein, referred to as NABP1 (nucleic-acid-binding protein 1). This subsequently led to the identification of an additional protein, closely related to NABP1, designated NABP2. Both proteins contain an OB (oligonucleotide/oligosaccharide binding) motif at their N-terminus. This motif is highly conserved between the two proteins. NABP1 is highly expressed in the thymus of wild-type mice and is greatly suppressed in RORγ−/− mice. During thymopoiesis, NABP1 mRNA expression is restricted to CD4+CD8+ thymocytes, an expression pattern similar to that observed for RORγ2. These observations appear to suggest that NABP1 expression is regulated either directly or indirectly by RORγ2. Confocal microscopic analysis showed that the NABP1 protein localizes to the nucleus. Analysis of nuclear proteins by size-exclusion chromatography indicated that NABP1 is part of a high molecular-mass protein complex. Since the OB-fold is frequently involved in the recognition of nucleic acids, the interaction of NABP1 with various nucleic acids was examined. Our results demonstrate that NABP1 binds single-stranded nucleic acids, but not double-stranded DNA, suggesting that it functions as a single-stranded nucleic acid binding protein.

Cellular nucleic-acid-binding protein, a transcriptional enhancer of c-Myc, promotes the formation of parallel G-quadruplexes

2010 ◽  
Vol 428 (3) ◽  
pp. 491-498 ◽  
Author(s):  
Mariana Borgognone ◽  
Pablo Armas ◽  
Nora B. Calcaterra
Keyword(s):  
Nucleic Acid ◽  
Molecular Mechanisms ◽  
Binding Protein ◽  
Nucleic Acid Binding ◽  
Transcriptional Enhancer ◽  
Mobility Shift ◽  
Nucleic Acid Binding Protein ◽  
Control Of Gene Expression ◽  
Acid Binding Protein ◽  
Nucleic Acid Chaperone

G-rich sequences that contain stretches of tandem guanines can form four-stranded, intramolecular stable DNA structures called G-quadruplexes (termed G4s). Regulation of the equilibrium between single-stranded and G4 DNA in promoter regions is essential for control of gene expression in the cell. G4s are highly stable structures; however, their folding kinetics are slow under physiological conditions. CNBP (cellular nucleic-acid-binding protein) is a nucleic acid chaperone that binds the G4-forming G-rich sequence located within the NHE (nuclease hypersensitivity element) III of the c-Myc proto-oncogene promoter. Several reports have demonstrated that CNBP enhances the transcription of c-Myc in vitro and in vivo; however, none of these reports have assessed the molecular mechanisms responsible for this control. In the present study, by means of Taq polymerase stop assays, electrophoretic mobility-shift assays and CD spectroscopy, we show that CNBP promotes the formation of parallel G4s to the detriment of anti-parallel G4s, and its nucleic acid chaperone activity is required for this effect. These findings are the first to implicate CNBP as a G4-folding modulator and, furthermore, assign CNBP a novel mode-of-action during c-Myc transcriptional regulation.

cDNA cloning and developmental expression of cellular nucleic acid-binding protein (CNBP) gene in Xenopus laevis

Gene ◽  
2000 ◽  
Vol 241 (1) ◽  
pp. 35-43 ◽  
Author(s):  
Alessandra De Dominicis ◽  
Francesco Lotti ◽  
Paola Pierandrei-Amaldi ◽  
Beatrice Cardinali
Keyword(s):  
Nucleic Acid ◽  
Xenopus Laevis ◽  
Cdna Cloning ◽  
Binding Protein ◽  
Developmental Expression ◽  
Nucleic Acid Binding ◽  
Nucleic Acid Binding Protein ◽  
Acid Binding Protein

scholarly journals brlA requires both zinc fingers to induce development.

1990 ◽  
Vol 10 (4) ◽  
pp. 1815-1817 ◽  
Author(s):  
T H Adams ◽  
H Deising ◽  
W E Timberlake
Keyword(s):  
Nucleic Acid ◽  
Aspergillus Nidulans ◽  
Binding Protein ◽  
Zinc Fingers ◽  
Nucleic Acid Binding ◽  
Developmental Pathway ◽  
Nucleic Acid Binding Protein ◽  
Acid Binding Protein ◽  
Coordination Sites ◽  
Brla Gene

Expression of the Aspergillus nidulans brlA gene induces a developmental pathway leading to the production of asexual spores. We have introduced mutations into brlA that are expected to disrupt either or both Cys2-His2 Zn(II) coordination sites postulated to exist in the BrlA polypeptide. The resultant brlA alleles fail to induce either the asexual reproductive pathway or the expression of development-specific genes. These data support the hypothesis that brlA encodes a nucleic acid-binding protein whose activity requires each of two zinc fingers.

Sign in / Sign up

Export Citation Format

Share Document