scholarly journals SetDB1 and Su(var)3-9 play non-overlapping roles in somatic cell chromosomes of Drosophila melanogaster

2020 ◽  
pp. jcs.253096
Author(s):  
Darya A. Kalashnikova ◽  
Daniil A. Maksimov ◽  
Stanislav E. Romanov ◽  
Petr P. Laktionov ◽  
Dmitry E. Koryakov
Keyword(s):  
Drosophila Melanogaster ◽  
Salivary Gland ◽  
Binding Sites ◽  
Poor Correlation ◽  
H3k9 Methylation ◽  
Repeated Dna ◽  
Binding Profile ◽  
Chromosomal Proteins ◽  
Histone Methyltransferases ◽  
Functional Roles

We explored functional roles of two H3K9-specific histone methyltransferases SetDB1 and Su(var)3-9. Using DamID approach, we generated the binding profile for SetDB1 in Drosophila salivary gland chromosomes, and matched it to the profile of Su(var)3-9. Unlike Su(var)3-9, SetDB1 turned out to be an euchromatic protein that is absent from repeated DNA compartment, and is largely restricted to TSSes and 5'UTRs of ubiquitously expressed genes. Significant SetDB1 association is also observed at insulator protein CP190 binding sites. SetDB1 and H3K9me2/3-enriched sites tend to display poor overlap. At the same time, SetDB1 has clear connection with the distribution of H3K27me3 mark. SetDB1 binds outside the domains possessing this modification, and about half of the borders of H3K27me3 domains are decorated by SetDB1 together with actively transcribed genes. On the basis of poor correlation between the distribution of SetDB1 and H3K9 methylation marks, we speculate that in somatic cells, SetDB1 may contribute to the methylation of a broader set of chromosomal proteins than just H3K9. In addition, SetDB1 can be expected to play a role in the establishment of chromatin functional domains.

scholarly journals Cytogenetic and complementation analyses of recessive lethal mutations induced in the X chromosome of Drosophila by three alkylating agents

1974 ◽  
Vol 24 (1) ◽  
pp. 1-10 ◽  
Author(s):  
J. K. Lim ◽  
L. A. Snyder
Keyword(s):  
Drosophila Melanogaster ◽  
Salivary Gland ◽  
X Chromosome ◽  
Alkylating Agents ◽  
Complementation Analysis ◽  
Ethyl Methanesulphonate ◽  
Induced Mutations ◽  
Recessive Lethal ◽  
Lethal Mutations

SUMMARYSalivary-gland chromosomes of 54 methyl methanesulphonate- and 50 triethylene melamine-induced X-chromosome recessive lethals in Drosophila melanogaster were analysed. Two of the lethals induced by the mono-functional agent and 11 of those induced by the polyfunctional agent were found to be associated with detectable aberrations. A complementation analysis was also done on 82 ethyl methanesulphonate- and 34 triethylene melamine-induced recessive lethals in the zeste-white region of the X chromosome. The EMS-induced lethals were found to represent lesions affecting only single cistrons. Each of the 14 cistrons in the region known to mutate to a lethal state was represented by mutant alleles, but in widely different frequencies. Seven of the TEM-induced lethals were associated with deletions, only one of which had both breakpoints within the mapped region. Twenty-six of the 27 mutations in which only single cistrons were affected were mapped to 7 of the 14 known loci. One TEM- and two EMS-induced mutations were alleles representing a previously undetected locus in the zeste-white region.

Drosophila melanogaster H1 histone is phosphorylated stably

1987 ◽  
Vol 7 (11) ◽  
pp. 4118-4121
Author(s):  
D A Talmage ◽  
M Blumenfeld
Keyword(s):  
Drosophila Melanogaster ◽  
Salivary Gland ◽  
Dna Replication ◽  
Cultured Cells ◽  
Phosphorylation Site ◽  
Developmentally Regulated ◽  
Central Domain ◽  
Salivary Gland Cells ◽  
Adult Head ◽  
The Relationship

Phosphorylation of histone H1 is developmentally regulated in Drosophila spp. It cannot be detected in preblastoderm embryos or polytene salivary gland cells, but in cellular blastoderm, postblastoderm embryo, and amitotic adult head nuclei, it occurs with a frequency of roughly 4 x 10(5) molecules per nucleus. We used pulse-labeling to study the relationship between H1 synthesis and modification in cultured cells. These results reveal that the H1-associated phosphate is stable and suggest that Drosophila H1 is synthesized, translocated to the nucleus, associated with chromatin, and then phosphorylated. Partial tryptic digestion of Drosophila H1 revealed that the phosphorylation site is located within the globular, central domain of the protein. Thus, the developmentally regulated phosphorylation of Drosophila H1 presents two contrasts with previously studied H1 phosphorylation. It is not correlated with DNA replication, and it is located in the central domain of the protein.

scholarly journals Targeting histone methylation for colorectal cancer

2016 ◽  
Vol 10 (1) ◽  
pp. 114-131 ◽  
Author(s):  
Tao Huang ◽  
Chengyuan Lin ◽  
Linda L. D. Zhong ◽  
Ling Zhao ◽  
Ge Zhang ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Histone Methylation ◽  
Therapeutic Effects ◽  
Epigenetic Alterations ◽  
Chemical Probes ◽  
Histone Methyltransferases ◽  
Functional Roles ◽  
Promising Target ◽  
Multiple Levels ◽  
Small Molecule Modulators

As a leading cause of cancer deaths worldwide, colorectal cancer (CRC) results from accumulation of both genetic and epigenetic alterations. Disruption of epigenetic regulation in CRC, particularly aberrant histone methylation mediated by histone methyltransferases (HMTs) and demethylases (HDMs), have drawn increasing interest in recent years. In this paper, we aim to review the roles of histone methylation and associated enzymes in the pathogenesis of CRC, and the development of small-molecule modulators to regulate histone methylation for treating CRC. Multiple levels of evidence suggest that aberrant histone methylations play important roles in CRC. More than 20 histone-methylation enzymes are found to be clinically relevant to CRC, including 17 oncoproteins and 8 tumor suppressors. Inhibitors of EZH2 and DOT1L have demonstrated promising therapeutic effects in preclinical CRC treatment. Potent and selective chemical probes of histone-methylation enzymes are required for validation of their functional roles in carcinogenesis and clinical translations as CRC therapies. With EZH2 inhibitor EPZ-6438 entering into phase I/II trials for advanced solid tumors, histone methylation is emerging as a promising target for CRC.

scholarly journals Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins

2008 ◽  
Vol 183 (4) ◽  
pp. 607-615 ◽  
Author(s):  
Rita Sinka ◽  
Alison K. Gillingham ◽  
Vangelis Kondylis ◽  
Sean Munro
Keyword(s):  
Drosophila Melanogaster ◽  
Golgi Apparatus ◽  
G Protein ◽  
G Proteins ◽  
Binding Sites ◽  
Coiled Coil ◽  
Multiple Binding Sites ◽  
Multiple Binding ◽  
Rab Family ◽  
First Contact

Vesicles and other carriers destined for the Golgi apparatus must be guided to the correct cisternae. Golgins, long coiled-coil proteins that localize to particular Golgi subdomains via their C termini, are candidate regulators of vesicle sorting. In this study, we report that the GRIP domain golgins, whose C termini bind the Arf-like 1 G protein on the trans-Golgi, can also bind four members of the Rab family of G proteins. The Rab2-, Rab6-, Rab19-, and Rab30-binding sites are within the coiled-coil regions that are not required for Golgi targeting. Binding sites for two of these Rabs are also present on two coiled-coil proteins of the cis-Golgi, the Drosophila melanogaster orthologues of GM130 and GMAP-210. We suggest an integrated model for a tentacular Golgi in which coiled-coil proteins surround the Golgi to capture and retain Rab-containing membranes, excluding other structures such as ribosomes. Binding sites for diverse Rabs could ensure that incoming carriers are captured on first contact and moved to their correct destination within the stack.

scholarly journals Functional Roles of the Non-Catalytic Calcium-Binding Sites in the N-Terminal Domain of Human Peptidylarginine Deiminase 4

PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e51660 ◽  
Author(s):  
Yi-Liang Liu ◽  
I-Chen Tsai ◽  
Chia-Wei Chang ◽  
Ya-Fan Liao ◽  
Guang-Yaw Liu ◽  
...  
Keyword(s):  
Binding Sites ◽  
Calcium Binding ◽  
Peptidylarginine Deiminase ◽  
Functional Roles ◽  
Peptidylarginine Deiminase 4 ◽  
Terminal Domain ◽  
Calcium Binding Sites

p75, a polypeptide component of karyoskeletal protein-enriched fractions associated with transcriptionally active loci of Drosophila melanogaster polytene chromosomes

1988 ◽  
Vol 8 (5) ◽  
pp. 1877-1886
Author(s):  
B M Benton ◽  
S Berrios ◽  
P A Fisher
Keyword(s):  
Tissue Culture ◽  
Drosophila Melanogaster ◽  
Transcriptional Regulation ◽  
Salivary Gland ◽  
Indirect Immunofluorescence ◽  
Polytene Chromosomes ◽  
Nuclear Interior ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Larval Salivary Gland

A 75-kilodalton polypeptide has been identified which copurifies with karyoskeletal protein-enriched fractions prepared from Drosophila melanogaster embryos. Results of indirect immunofluorescence experiments suggest that this protein, here designated p75, is primarily associated with puffed regions of larval salivary gland polytene chromosomes. In nonpolytenized Schneider 2 tissue culture cells, p75 appeared to be localized throughout the nuclear interior during interphase. In mitotic cells, p75 was redistributed diffusely. A possible role for karyoskeletal elements in transcriptional regulation is discussed.

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