Benzo(a)pyrene diol epoxides as intermediates in nucleic acid binding in vitro and in vivo

Science ◽  
1976 ◽  
Vol 193 (4253) ◽  
pp. 592-595 ◽  
Author(s):  
I. Weinstein ◽  
A. Jeffrey ◽  
K. Jennette ◽  
S. Blobstein ◽  
R. Harvey ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acid Binding ◽  
Diol Epoxides

ChemInform Abstract: BENZO(A)PYRENE DIOL EPOXIDES AS INTERMEDIATES IN NUCLEIC ACID BINDING IN VITRO AND IN VIVO

1976 ◽  
Vol 7 (49) ◽  
pp. no-no
Author(s):  
I. B. WEINSTEIN ◽  
A. M. JEFFREY ◽  
K. W. JENNETTE ◽  
S. H. BLOBSTEIN ◽  
R. G. HARVEY ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acid Binding ◽  
Diol Epoxides

scholarly journals The Gly/Arg-rich (GAR) domain of Xenopus nucleolin facilitates in vitro nucleic acid binding and in vivo nucleolar localization.

1993 ◽  
Vol 4 (11) ◽  
pp. 1189-1204 ◽  
Author(s):  
M A Heine ◽  
M L Rankin ◽  
P J DiMario
Keyword(s):  
Nucleic Acid ◽  
Binding Activity ◽  
Full Length ◽  
Nucleic Acid Binding ◽  
Binding Assays ◽  
Nucleic Acid Probes ◽  
E Coli ◽  
Indirect Immunofluorescence Staining

Epitope-tagged Xenopus nucleolin was expressed in Escherichia coli cells and in Xenopus oocytes either as a full-length wild-type protein or as a truncation that lacked the distinctive carboxy glycine/arginine-rich (GAR) domain. Both full-length and truncated versions of nucleolin were tagged at their amino termini with five tandem human c-myc epitopes. Whether produced in E. coli or in Xenopus, epitope-tagged full-length nucleolin bound nucleic acid probes in in vitro filter binding assays. Conversely, the E. coli-expressed GAR truncation failed to bind the nucleic acid probes, whereas the Xenopus-expressed truncation maintained slight binding activity. Indirect immunofluorescence staining showed that myc-tagged full-length nucleolin properly localized to the dense fibrillar regions within the multiple nucleoli of Xenopus oocyte nuclei. The epitope-tagged GAR truncation also translocated to the oocyte nuclei, but it failed to efficiently localize to the nucleoli. Our results show that the carboxy GAR domain must be present for nucleolin to efficiently bind nucleic acids in vitro and to associate with nucleoli in vivo.

Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix protein which binds DNA and RNA in vivo and in vitro

1994 ◽  
Vol 221 (2) ◽  
pp. 749-757 ◽  
Author(s):  
Frank O. FACKELMAYER ◽  
Kirsten DAHM ◽  
Andrea RENZ ◽  
Uwe RAMSPERGER ◽  
Arndt RICHTER
Keyword(s):  
Nucleic Acid ◽  
Nuclear Matrix ◽  
Matrix Protein ◽  
Nucleic Acid Binding ◽  
Nuclear Matrix Protein ◽  
Binding Properties ◽  
Dna And Rna ◽  
Hnrnp U

scholarly journals Structural basis of nucleic-acid recognition and double-strand unwinding by the essential neuronal protein Pur-alpha

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Janine Weber ◽  
Han Bao ◽  
Christoph Hartlmüller ◽  
Zhiqin Wang ◽  
Almut Windhager ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nucleic Acid ◽  
Molecular Mechanisms ◽  
Rna Binding ◽  
Point Mutations ◽  
Structural Basis ◽  
Binding Modes ◽  
Nucleic Acid Binding

The neuronal DNA-/RNA-binding protein Pur-alpha is a transcription regulator and core factor for mRNA localization. Pur-alpha-deficient mice die after birth with pleiotropic neuronal defects. Here, we report the crystal structure of the DNA-/RNA-binding domain of Pur-alpha in complex with ssDNA. It reveals base-specific recognition and offers a molecular explanation for the effect of point mutations in the 5q31.3 microdeletion syndrome. Consistent with the crystal structure, biochemical and NMR data indicate that Pur-alpha binds DNA and RNA in the same way, suggesting binding modes for tri- and hexanucleotide-repeat RNAs in two neurodegenerative RNAopathies. Additionally, structure-based in vitro experiments resolved the molecular mechanism of Pur-alpha's unwindase activity. Complementing in vivo analyses in Drosophila demonstrated the importance of a highly conserved phenylalanine for Pur-alpha's unwinding and neuroprotective function. By uncovering the molecular mechanisms of nucleic-acid binding, this study contributes to understanding the cellular role of Pur-alpha and its implications in neurodegenerative diseases.

scholarly journals The MRG Domain Mediates the Functional Integration of MSL3 into the Dosage Compensation Complex

2005 ◽  
Vol 25 (14) ◽  
pp. 5947-5954 ◽  
Author(s):  
Violette Morales ◽  
Catherine Regnard ◽  
Annalisa Izzo ◽  
Irene Vetter ◽  
Peter B. Becker
Keyword(s):  
Nucleic Acid ◽  
X Chromosome ◽  
Dosage Compensation ◽  
De Novo ◽  
Functional Integration ◽  
Binding Activity ◽  
Nucleic Acid Binding ◽  
Dosage Compensation Complex

ABSTRACT The male-specific-lethal (MSL) proteins in Drosophila melanogaster serve to adjust gene expression levels in male flies containing a single X chromosome to equal those in females with a double dose of X-linked genes. Together with noncoding roX RNA, MSL proteins form the “dosage compensation complex” (DCC), which interacts selectively with the X chromosome to restrict the transcription-activating histone H4 acetyltransferase MOF (males-absent-on-the-first) to that chromosome. We showed previously that MSL3 is essential for the activation of MOF's nucleosomal histone acetyltransferase activity within an MSL1-MOF complex. By characterizing the MSL3 domain structure and its associated functions, we now found that the nucleic acid binding determinants reside in the N terminus of MSL3, well separable from the C-terminal MRG signatures that form an integrated domain required for MSL1 interaction. Interaction with MSL1 mediates the activation of MOF in vitro and the targeting of MSL3 to the X-chromosomal territory in vivo. An N-terminal truncation that lacks the chromo-related domain and all nucleic acid binding activity is able to trigger de novo assembly of the DCC and establishment of an acetylated X-chromosome territory.

IMMU-53. STING-ING GLIOBLASTOMA WITH SPHERICAL NUCLEIC ACIDS

2021 ◽  
Vol 23 (Supplement_6) ◽  
pp. vi104-vi105
Author(s):  
Akanksha Mahajan ◽  
Lisa Hurley ◽  
Serena Tommasini-Ghelfi ◽  
Corey Dussold ◽  
Alexander Stegh ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
High Surface ◽  
Biological Properties ◽  
Innate Immune ◽  
Limiting Factors ◽  
Nucleic Acid Delivery ◽  
Sting Pathway ◽  
Spherical Nucleic Acids

Abstract The Stimulator of Interferon Genes (STING) pathway represents a major innate immune sensing mechanism for tumor-derived DNA. Modified cyclic dinucleotides (CDNs) that mimic the endogenous STING ligand cGAMP are currently being explored in patients with solid tumors that are amenable to intratumoral delivery. Inadequate bioavailability and insufficient lipophilicity are limiting factors for clinical CDN development, in particular when consideration is given to systemic administration approaches. We have shown that the formulation of oligonucleotides into Spherical Nucleic Acid (SNA) nanostructures, i.e.,the presentation of oligonucleotides at high density on the surface of nanoparticle cores, lead to biochemical and biological properties that are radically different from those of linear oligonucleotides. First-generation brain-penetrant siRNA-based SNAs (NCT03020017, recurrent GBM) have recently completed early clinical trials. Here, we report the development of a STING-agonistic immunotherapy by targeting cGAS, the sensor of cytosolic dsDNA upstream of STING, with SNAs presenting dsDNA at high surface density. The strategy of using SNAs exploits the ability of cGAS to raise STING responses by delivering dsDNA and inducing the catalytic production of endogenous CDNs. SNA nanostructures carrying a 45bp IFN-simulating dsDNA oligonucleotide, the most commonly used and widely characterized cGAS activator, potently activated the cGAS-STING pathway in vitro and in vivo. In a poorly immunogenic and highly aggressive syngeneic mouse glioma model, in which tumours were well-established, only one dose of intranasal treatment with STING-SNAs decelerated tumour growth, improved survival and importantly, was well-tolerated. Our use of SNAs addresses the challenges of nucleic acid delivery to intracranial tumor sites via intranasal route, exploits the binding of dsDNA molecules on the SNA surface to enhance the formation of a dimeric cGAS:DNA complex and establishes cGAS-agonistic SNAs as a novel class of immune-stimulatory modalities for triggering innate immune responses against tumor.

Framework nucleic acid programmed combinatorial delivery nanocarriers for parallel and multiplexed analysis

2021 ◽  
Author(s):  
Yinghui Feng ◽  
Qi Liu ◽  
Miao Chen ◽  
Xinyi Zhao ◽  
Lumin Wang ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Multiplexed Analysis

Herein we report a framework nucleic acid programmed strategy to develop nanocarriers to precisely and independently package multiple homo- and heterogeneous cargos in vitro and in vivo, thereby enabling multiplexed...

1,4-Butanediol diglycidyl ether (BDE)-crosslinked PEI-g-imidazole nanoparticles as nucleic acid-carriers in vitro and in vivo

2011 ◽  
Vol 7 (6) ◽  
pp. 2055 ◽  
Author(s):  
Ritu Goyal ◽  
Ruby Bansal ◽  
Shilpa Tyagi ◽  
Yogeshwer Shukla ◽  
Pradeep Kumar ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Diglycidyl Ether

Regulation der Chlorophyllbiosynthese. Lidit- und entwicklungsbedingte Aktivitätsänderungen von vier aufeinander folgenden Enzymen der Porphyrin- und Chlorophyllbiosynthesekette / Regulation of Chlorophyll Biosynthesis. Changes in Activity of Four Consecutive Enzymes in the Porphyrin and Chlorophyll Biosynthesis Chain during Development and Illumination

1973 ◽  
Vol 28 (1-2) ◽  
pp. 45-58 ◽  
Author(s):  
Hansjörg A. W. Schneider
Keyword(s):  
Nucleic Acid ◽  
Chlorophyll Biosynthesis ◽  
Acid Synthesis ◽  
Chlorophyll Synthesis ◽  
The Other ◽  
Tissue Cultures ◽  
Leaf Tissues ◽  
Porphyrin Synthesis

The activities of enzymes related with chlorophyll and porphyrin synthesis have been examined during development and greening of young corn leaves. The enzymes succinyl-CoA-synthetase (SCoAS), δ-amino-levulinate synthetase (ALAS), δ-amino-levulinate dehydratase (ALAD) and the enzymes involved in porphobilinogenase (PBGA) were under investigaton. When leaves are illuminated and chlorophyll synthesis begins the activity of ALAD is not influenced. The activity of PBGA and SCoAS are slightly higher than in darkness, but the changes are below the range affecting chlorophyll biosynthesis. ALA, however, is only synthetized in the light. Synthesis ceases immediately when illuminiation ist stopped, indicating'that in darkness ALAS is not active. On the other hand ALAS is active in dark grown roots, tubers and other non-leaf tissues. Feeding the plant with succinate, glycine or α-keto-glutarate has no effect on chlorophyll synthesis, but the amount of ALA is reduced, whereas sucrose promotes its accumulation. The results are discussed with completely antitethaal results obtained with tissue cultures of tobacco and are integrated into a scheme which excludes the contrariety of hypotheses deduced from experi- ments with inhibitors of protein and nucleic acid synthesis. It is suggested that the varying results are caused by the action of light on different stages in differentiation of plastids and cells. In contrast to the enzymes SCoAS, ALAD and PBGA whose activities were determined in vitro, ALAS was assayed in vivo by means of the accumulation of (5-amino-levulinate (ALA) after blocking the enzyme ALAD by levulinate (LA). Optimum accumulation is observed when the concentration is about 2 · 10-2 м. LA is not converted to ALA in appreciable amounts. This could be proved by feeding the plants with 14C-LA which was prepared from uniformly labeled 14C-fructose.

Sign in / Sign up

Export Citation Format

Share Document