In-Nucleus Hi-C in Drosophila Cells

10.3791/62106 ◽  
2021 ◽  
Author(s):  
Ayerim Esquivel-López ◽  
Rodrigo Arzate-Mejía ◽  
Rosario Pérez-Molina ◽  
Mayra Furlan-Magaril
Keyword(s):  
Drosophila Cells

scholarly journals Visual4DTracker: a tool to interact with 3D + t image stacks

2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Ermanno Cordelli ◽  
Paolo Soda ◽  
Giulio Iannello
Keyword(s):  
Synthetic Data ◽  
Time Lapse ◽  
Temporal Data ◽  
Image Stack ◽  
Biological Phenomena ◽  
Insulin Granules ◽  
Matlab Package ◽  
User Friendly ◽  
Drosophila Cells ◽  
Over Time

Abstract Background Biological phenomena usually evolves over time and recent advances in high-throughput microscopy have made possible to collect multiple 3D images over time, generating $$3D+t$$ 3 D + t (or 4D) datasets. To extract useful information there is the need to extract spatial and temporal data on the particles that are in the images, but particle tracking and feature extraction need some kind of assistance. Results This manuscript introduces our new freely downloadable toolbox, the Visual4DTracker. It is a MATLAB package implementing several useful functionalities to navigate, analyse and proof-read the track of each particle detected in any $$3D+t$$ 3 D + t stack. Furthermore, it allows users to proof-read and to evaluate the traces with respect to a given gold standard. The Visual4DTracker toolbox permits the users to visualize and save all the generated results through a user-friendly graphical user interface. This tool has been successfully used in three applicative examples. The first processes synthetic data to show all the software functionalities. The second shows how to process a 4D image stack showing the time-lapse growth of Drosophila cells in an embryo. The third example presents the quantitative analysis of insulin granules in living beta-cells, showing that such particles have two main dynamics that coexist inside the cells. Conclusions Visual4DTracker is a software package for MATLAB to visualize, handle and manually track $$3D+t$$ 3 D + t stacks of microscopy images containing objects such cells, granules, etc.. With its unique set of functions, it remarkably permits the user to analyze and proof-read 4D data in a friendly 3D fashion. The tool is freely available at https://drive.google.com/drive/folders/19AEn0TqP-2B8Z10kOavEAopTUxsKUV73?usp=sharing

scholarly journals DIFFERENTIATION OF DROSOPHILA CELLS LACKING RIBOSOMAL DNA, IN VITRO

Genetics ◽  
1973 ◽  
Vol 73 (3) ◽  
pp. 429-434
Author(s):  
J James Donady ◽  
R L Seecof ◽  
M A Fox
Keyword(s):  
Drosophila Melanogaster ◽  
Ribosomal Rna ◽  
Ribosomal Dna ◽  
Rna Synthesis ◽  
Wild Type ◽  
Drosophila Cells

ABSTRACT Drosophila melanogaster embryos that lacked ribosomal DNA were obtained from appropriate crosses. Cells were taken from such embryos before overt differentiation took place and were cultured in vitro. These cells differentiated into neurons and myocytes with the same success as did wild-type controls. Therefore, ribosomal RNA synthesis is not necessary for the differentiation of neurons and myocytes in vitro.

scholarly journals Drosophila CG2469 Encodes a Homolog of Human CTR9 and Is Essential for Development

2016 ◽  
Vol 6 (12) ◽  
pp. 3849-3857 ◽  
Author(s):  
Dhananjay Chaturvedi ◽  
Mayu Inaba ◽  
Shane Scoggin ◽  
Michael Buszczak
Keyword(s):  
Germ Cell ◽  
Sequence Similarity ◽  
Cell Loss ◽  
Germline Stem Cell ◽  
Cell Nuclei ◽  
Transcriptional Initiation ◽  
Histone Locus Bodies ◽  
Paf1 Complex ◽  
Histone Locus ◽  
Drosophila Cells

Abstract Conserved from yeast to humans, the Paf1 complex participates in a number of diverse processes including transcriptional initiation and polyadenylation. This complex typically includes five proteins: Paf1, Rtf1, Cdc73, Leo1, and Ctr9. Previous efforts identified clear Drosophila homologs of Paf1, Rtf1, and Cdc73 based on sequence similarity. Further work showed that these proteins help to regulate gene expression and are required for viability. To date, a Drosophila homolog of Ctr9 has remained uncharacterized. Here, we show that the gene CG2469 encodes a functional Drosophila Ctr9 homolog. Both human and Drosophila Ctr9 localize to the nuclei of Drosophila cells and appear enriched in histone locus bodies. RNAi knockdown of Drosophila Ctr9 results in a germline stem cell loss phenotype marked by defects in the morphology of germ cell nuclei. A molecular null mutation of Drosophila Ctr9 results in lethality and a human cDNA CTR9 transgene rescues this phenotype. Clonal analysis in the ovary using this null allele reveals that loss of Drosophila Ctr9 results in a reduction of global levels of histone H3 trimethylation of lysine 4 (H3K4me3), but does not compromise the maintenance of stem cells in ovaries. Given the differences between the null mutant and RNAi knockdown phenotypes, the germ cell defects caused by RNAi likely result from the combined loss of Drosophila Ctr9 and other unidentified genes. These data provide further evidence that the function of this Paf1 complex component is conserved across species.

Drosophila Cells in Culture

1999 ◽  
Vol 23 (9) ◽  
pp. 651
Author(s):  
S Saunders
Keyword(s):  
Cells In Culture ◽  
Drosophila Cells

The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA

1992 ◽  
Vol 12 (8) ◽  
pp. 3390-3398
Author(s):  
A Blanc ◽  
C Goyer ◽  
N Sonenberg
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Coat Protein ◽  
Translation Initiation ◽  
Rna Virus ◽  
Binding Protein ◽  
Covalent Bond ◽  
Cellular Proteins ◽  
Double Stranded Rna ◽  
Virus Coat ◽  
Drosophila Cells

The eukaryotic mRNA 5' cap structure m7GpppX (where X is any nucleotide) interacts with a number of cellular proteins. Several of these proteins were studied in mammalian, yeast, and drosophila cells and found to be involved in translation initiation. Here we describe a novel cap-binding protein, the coat protein of L-A, a double-stranded RNA virus that is persistently maintained in many Saccharomyces cerevisiae strains. The results also suggest that the coat protein of a related double-stranded RNA virus (L-BC) is likewise a cap-binding protein. Strikingly, in contrast to the cellular cap-binding proteins, the interaction between the L-A virus coat protein and the cap structure is through a covalent bond.

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