scholarly journals Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS

Nature ◽  
1995 ◽  
Vol 376 (6537) ◽  
pp. 279-279 ◽  
Author(s):  
Xiuqu Qian ◽  
ChoonJu Jeon ◽  
HoSup Yoon ◽  
Kan Agarwal ◽  
Michael A. Weiss
Keyword(s):  
Nucleic Acid ◽  
Elongation Factor ◽  
Binding Motif ◽  
Transcriptional Elongation ◽  
Nucleic Acid Binding

scholarly journals Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS

Nature ◽  
1993 ◽  
Vol 365 (6443) ◽  
pp. 277-279 ◽  
Author(s):  
Xiuqu Qian ◽  
ChoonJu Jeon ◽  
HoSup Yoon ◽  
Kan Agarwal ◽  
Michael A. Weiss
Keyword(s):  
Nucleic Acid ◽  
Elongation Factor ◽  
Binding Motif ◽  
Transcriptional Elongation ◽  
Nucleic Acid Binding

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.

scholarly journals Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif

1987 ◽  
Vol 15 (12) ◽  
pp. 4771-4787 ◽  
Author(s):  
Thierry Grange ◽  
Cezar Martins de Sa ◽  
Jacqueline Oddos ◽  
Raymond Pictet
Keyword(s):  
Nucleic Acid ◽  
Binding Protein ◽  
Evolutionary Conservation ◽  
Binding Motif ◽  
Nucleic Acid Binding

scholarly journals Crystal structure and functional characterization of the human RBM25 PWI domain and its flanking basic region

2013 ◽  
Vol 450 (1) ◽  
pp. 85-94 ◽  
Author(s):  
Deshun Gong ◽  
Fan Yang ◽  
Fudong Li ◽  
Dandan Qian ◽  
Minhao Wu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Alternative Splicing ◽  
Nucleic Acid ◽  
Rna Binding ◽  
Functional Characterization ◽  
Binding Motif ◽  
Nucleic Acid Binding ◽  
Binding Surface ◽  
Basic Region

Human RBM25 (RNA-binding motif protein 25) is a novel splicing factor that contains a PWI domain, a newly identified RNA/DNA-binding domain, and regulates Bcl-x pre-mRNA alternative splicing. The flanking basic region has been suggested to serve as a co-operative partner of the PWI domain in the binding of nucleic acids, but the structure of this basic region is unknown. In the present paper, we report the crystal structure of the RBM25 PWI domain and its flanking basic region. The PWI domain is revealed to comprise a conserved four-helix bundle, and the flanking basic region forms two α-helices and associates with helix H4 of the PWI domain. These interactions promote directly the formation of an enlarged nucleic-acid-binding platform. Structure-guided mutagenesis reveals a positively charged nucleic-acid-binding surface in the RBM25 PWI domain that is entirely different from that in the SRm160 PWI domain. Furthermore, we show that the promotion of the pro-apoptotic Bcl-xS isoform expression by RBM25 is facilitated by the PWI domain in vivo. Thus the present study suggests that the PWI domain plays an important role in the regulation of Bcl-x pre-mRNA alternative splicing.

Snapshot blotting: The transfer of nucleic acids and nucleoprotein complexes from electrophoresis gels to EM grids

1992 ◽  
Vol 50 (1) ◽  
pp. 762-763
Author(s):  
Stephen D. Jett
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Nucleic Acid Binding ◽  
Mobility Shift ◽  
Carbon Coated ◽  
Nucleoprotein Complexes ◽  
Mobility Shift Assay ◽  
Protein Nucleic Acid ◽  
Gel Mobility Shift ◽  
Nucleic Acid Interactions

The electrophoresis gel mobility shift assay is a popular method for the study of protein-nucleic acid interactions. The binding of proteins to DNA is characterized by a reduction in the electrophoretic mobility of the nucleic acid. Binding affinity, stoichiometry, and kinetics can be obtained from such assays; however, it is often desirable to image the various species in the gel bands using TEM. Present methods for isolation of nucleoproteins from gel bands are inefficient and often destroy the native structure of the complexes. We have developed a technique, called “snapshot blotting,” by which nucleic acids and nucleoprotein complexes in electrophoresis gels can be electrophoretically transferred directly onto carbon-coated grids for TEM imaging.

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