Gentaur Pub

#29681056   // Save this To Up

A cytological approach to study meiotic recombination and chromosome dynamics of Arabidopsis thaliana male meiocytes in three dimensions.

During meiotic prophase I chromosomes undergo dramatic conformational changes that accompany chromosome condensation, pairing and recombination between homologs. These changes include the anchoring of telomeres to the nuclear envelope and their clustering to form a bouquet. In plants, these events have been studied and illustrated in intact meiocytes of large genome species. Arabidopsis thaliana is an excellent genetic model where major molecular pathways that control synapsis and recombination between homologs have been uncovered. Yet the study of chromosome dynamics is hampered by current cytological methods that disrupt the 3D architecture of the nucleus. Here we set up a protocol to preserve the 3D configuration of A. thaliana meiocytes. We showed that this technique is compatible with the use of a variety of antibodies that label structural and recombination proteins and were able to highlight the presence of clustered synapsis initiation centers at the nuclear periphery. By using fluorescence in situ hybridization (FISH) we also studied chromosome behavior during premeiotic G2 and prophase I, revealing the existence of a telomere bouquet during A. thaliana male meiosis. In addition we showed that the number of telomeres in a bouquet and its volume vary greatly thus revealing the complexity of telomere behavior during meiotic prophase I. Finally, by using probes that label subtelomeric regions of individual chromosomes we revealed differential localization behaviors of chromosome ends. Our protocol opens new areas of research to investigate chromosome dynamics in A. thaliana meiocytes. This article is protected by copyright. All rights reserved.

2209 related Products with: A cytological approach to study meiotic recombination and chromosome dynamics of Arabidopsis thaliana male meiocytes in three dimensions.

DNA (cytosine 5) methyltr Recombinant Human Interfe Cell Meterâ„¢ Fluorimetri Cell Meterâ„¢ Fluorimetri Homogenizer for 24 sample Top five cancer tissue ar Goat Anti-Human TOM1L1 SR FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Rabbit Anti-Human Toll In

Related Pathways

#29670105   // Save this To Up

Viral proteins as a potential driver of histone depletion in dinoflagellates.

Within canonical eukaryotic nuclei, DNA is packaged with highly conserved histone proteins into nucleosomes, which facilitate DNA condensation and contribute to genomic regulation. Yet the dinoflagellates, a group of unicellular algae, are a striking exception to this otherwise universal feature as they have largely abandoned histones and acquired apparently viral-derived substitutes termed DVNPs (dinoflagellate-viral-nucleoproteins). Despite the magnitude of this transition, its evolutionary drivers remain unknown. Here, using Saccharomyces cerevisiae as a model, we show that DVNP impairs growth and antagonizes chromatin by localizing to histone binding sites, displacing nucleosomes, and impairing transcription. Furthermore, DVNP toxicity can be relieved through histone depletion and cells diminish their histones in response to DVNP expression suggesting that histone reduction could have been an adaptive response to these viral proteins. These findings provide insights into eukaryotic chromatin evolution and highlight the potential for horizontal gene transfer to drive the divergence of cellular systems.

1398 related Products with: Viral proteins as a potential driver of histone depletion in dinoflagellates.

EpiQuik Histone Methyltra EpiQuik Histone Methyltra EpiQuik Histone Methyltra EpiQuik Histone Methyltra EpiQuik Histone Methyltra EpiQuik Histone Methyltra EMAP-II Inhibitor Z-ASTD- EMAP-II Inhibitor Z-ASTD- EMAP II Inhibitor Z ASTD EMAP II Inhibitor Z ASTD Ampliteâ„¢ Fluorimetric H Ampliteâ„¢ Intracellular

Related Pathways

#29669830   // Save this To Up

Evolution-guided structural and functional analyses of the HERC family reveals an ancient marine origin and determinants of antiviral activity.

In humans, 'homologous to the E6-AP carboxyl terminus (HECT) and regulator of chromosome condensation 1 (RCC1)-like domain-containing protein 5' (HERC5) is an interferon-induced protein that inhibits replication of evolutionarily diverse viruses including human immunodeficiency virus type 1 (HIV-1). To better understand the origin, evolution and function of HERC5, we performed phylogenetic, structural and functional analyses of the entire human small HERC family, which includes HERC3, HERC4, HERC5 and HERC6. We demonstrated that the family emerged >595 million years ago and has undergone gene duplication and gene loss events throughout its evolution. The structural topology of the RCC1-like domain and HECT domains from all HERC paralogs are highly conserved among evolutionarily diverse vertebrates despite low sequence homology. Functional analyses showed that the human small HERCs exhibit different degrees of antiviral activity towards HIV-1 and that HERC5 provided the strongest level of inhibition. Notably, coelacanth HERC5 inhibited SIV, but not HIV-1, particle production suggesting that the antiviral activity of HERC5 emerged over 413 million years ago and exhibits species- and virus-specific restriction. In addition, we showed that both HERC5 and HERC6 are evolving under strong positive selection; particularly blade 1 of the RCC1-like domain, which we showed is a key determinant of antiviral activity. These studies provide insight into the origin, evolution and biological importance of the human restriction factor HERC5 and the other HERC family members. Intrinsic immunity plays an important role as the first line of defense against viruses. Studying the origin, evolution and function of proteins responsible for effecting this defense will provide key information about virus-host relationships that can be exploited for future drug development. We showed that HERC5 is one such antiviral protein that belongs to an evolutionarily conserved family of HERCs with an ancient marine origin. Not all vertebrates possess all HERC members, suggesting that different HERCs emerged at different times during evolution to provide the host with a survival advantage. Consistent with this, some of the more recently emerged HERC members, HERC5 and HERC6, displayed strong signatures of having been involved in an ancient evolutionary battle with viruses. Our findings provide new insights into the evolutionary origin and function of the HERC family in vertebrate evolution, identifying HERC5 and possibly HERC6 as important effectors of intrinsic immunity in vertebrates.

1232 related Products with: Evolution-guided structural and functional analyses of the HERC family reveals an ancient marine origin and determinants of antiviral activity.

Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650 Primary antibody IL-1RAc Primary antibody IL-1RAc AZD-3514 Mechanisms: Andr 17β-Acetoxy-2α-bromo-5Π(5α,16β)-N-Acetyl-16-[2 (5α,16β)-N-Acetyl-16-ac 5α-N-Acetyl-2'H-androst-

Related Pathways

#29668347   // Save this To Up

Hypothermia modulates the DNA damage response to ionising radiation in human peripheral blood lymphocytes.

Low temperature at exposure has been shown to act in a radioprotective manner at the level of cytogenetic damage. It was suggested to be due to an effective transformation of DNA damage to chromosomal damage at low temperature. The purpose of the study was to analyse the kinetics of aberration formation during the first hours after exposing human peripheral blood lymphocytes to ionising radiation at 0.8 °C and 37 °C.

2219 related Products with: Hypothermia modulates the DNA damage response to ionising radiation in human peripheral blood lymphocytes.

Anti beta3 AR Human, Poly AccuPrep Genomic DNA Extr anti H inh human blood an Recombinant Human Interfe Goat Anti-Human TOM1L1 SR FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Rabbit Anti-Human Toll In Mouse Anti-Human CD103 (I Mouse Anti-Human CD103 (I

Related Pathways

#29657864   // Save this To Up

A Sequence-Dependent DNA Condensation Induced by Prion Protein.

Different studies indicated that the prion protein induces hybridization of complementary DNA strands. Cell culture studies showed that the scrapie isoform of prion protein remained bound with the chromosome. In present work, we used an oxazole dye, YOYO, as a reporter to quantitative characterization of the DNA condensation by prion protein. We observe that the prion protein induces greater fluorescence quenching of YOYO intercalated in DNA containing only GC bases compared to the DNA containing four bases whereas the effect of dye bound to DNA containing only AT bases is marginal. DNA-condensing biological polyamines are less effective than prion protein in quenching of DNA-bound YOYO fluorescence. The prion protein induces marginal quenching of fluorescence of the dye bound to oligonucleotides, which are resistant to condensation. The ultrastructural studies with electron microscope also validate the biophysical data. The GC bases of the target DNA are probably responsible for increased condensation in the presence of prion protein. To our knowledge, this is the first report of a human cellular protein inducing a sequence-dependent DNA condensation. The increased condensation of GC-rich DNA by prion protein may suggest a biological function of the prion protein and a role in its pathogenesis.

2802 related Products with: A Sequence-Dependent DNA Condensation Induced by Prion Protein.

DNA Binding Protein 7 (DB Mouse 3 mA DNA Glycosylas Mouse 3 mA DNA Glycosylas removed without changing Rabbit Anti-IEX1 Differen Rabbit Anti-IEX1 Differen Rabbit Anti-IEX1 Differen Rabbit Anti-IEX1 Differen Rabbit Anti-IEX1 Differen Rabbit Anti-IEX1 Differen Rabbit Anti-IEX1 Differen Rabbit Anti-IEX1 Differen

Related Pathways

#29618731   // Save this To Up

Plasmodium APC3 mediates chromosome condensation and cytokinesis during atypical mitosis in male gametogenesis.

The anaphase promoting complex/cyclosome (APC/C) is a highly conserved multi-subunit E3 ubiquitin ligase that controls mitotic division in eukaryotic cells by tagging cell cycle regulators for proteolysis. APC3 is a key component that contributes to APC/C function. Plasmodium, the causative agent of malaria, undergoes atypical mitotic division during its life cycle. Only a small subset of APC/C components has been identified in Plasmodium and their involvement in atypical cell division is not well understood. Here, using reverse genetics we examined the localisation and function of APC3 in Plasmodium berghei. APC3 was observed as a single focus that co-localised with the centriolar plaque during asexual cell division in schizonts, whereas it appeared as multiple foci in male gametocytes. Functional studies using gene disruption and conditional knockdown revealed essential roles of APC3 during these mitotic stages with loss resulting in a lack of chromosome condensation, abnormal cytokinesis and absence of microgamete formation. Overall, our data suggest that Plasmodium utilises unique cell cycle machinery to coordinate various processes during endomitosis, and this warrants further investigation in future studies.

1725 related Products with: Plasmodium APC3 mediates chromosome condensation and cytokinesis during atypical mitosis in male gametogenesis.

DNA (cytosine 5) methyltr Tide Fluorâ„¢ 8 maleimide Mouse Anti-Plasmodium fal Esophageal inflammation, Male genitourinary system Anti-ACIN1ACIN1(Apoptotic Anti ACIN1ACIN1(Apoptotic Interleukin-34 IL34 (N-t Interleukin-34 IL34 anti Sterile filtered goat se Sterile filtered goat se Sterile filtered mouse s

Related Pathways

#29563586   // Save this To Up

JMJD5 is a human arginyl C-3 hydroxylase.

Oxygenase-catalysed post-translational modifications of basic protein residues, including lysyl hydroxylations and N-methyl lysyl demethylations, have important cellular roles. Jumonji-C (JmjC) domain-containing protein 5 (JMJD5), which genetic studies reveal is essential in animal development, is reported as a histone N-methyl lysine demethylase (KDM). Here we report how extensive screening with peptides based on JMJD5 interacting proteins led to the finding that JMJD5 catalyses stereoselective C-3 hydroxylation of arginine residues in sequences from human regulator of chromosome condensation domain-containing protein 1 (RCCD1) and ribosomal protein S6 (RPS6). High-resolution crystallographic analyses reveal overall fold, active site and substrate binding/product release features supporting the assignment of JMJD5 as an arginine hydroxylase rather than a KDM. The results will be useful in the development of selective oxygenase inhibitors for the treatment of cancer and genetic diseases.

2178 related Products with: JMJD5 is a human arginyl C-3 hydroxylase.

Rabbit Anti-Tyrosine Hydr Mouse Anti-beta-Amyloid(1 Rabbit Anti-beta-Amyloid( Rabbit Anti-Nociceptin re Rabbit Anti-14-3-3(Alpha Rabbit Anti-factor VIII(F Rabbit Anti-TSLP (human) Rabbit Anti-EpCAM CD326 P Rabbit Anti-GCK Glucokina Rabbit Anti-GPR78 Polyclo Rabbit Anti-RYBP APAP1 CD Rabbit Anti-Nkx2.5 Cardia

Related Pathways

#29533658   // Save this To Up

Interrogation of Benzomalvin Biosynthesis Using Fungal Artificial Chromosomes with Metabolomic Scoring (FAC-MS): Discovery of a Benzodiazepine Synthase Activity.

The benzodiazepine benzomalvin A/D is a fungally derived specialized metabolite and inhibitor of the substance P receptor NK1, biosynthesized by a three-gene nonribosomal peptide synthetase cluster. Here, we utilize fungal artificial chromosomes with metabolomic scoring (FAC-MS) to perform molecular genetic pathway dissection and targeted metabolomics analysis to assign the in vivo role of each domain in the benzomalvin biosynthetic pathway. The use of FAC-MS identified the terminal cyclizing condensation domain as BenY-C and the internal C-domains as BenZ-C and BenZ-C. Unexpectedly, we also uncovered evidence suggesting BenY-C or a yet to be identified protein mediates benzodiazepine formation, representing the first reported benzodiazepine synthase enzymatic activity. This work informs understanding of what defines a fungal C domain and shows how the FAC-MS platform can be used as a tool for in vivo analyses of specialized metabolite biosynthesis and for the discovery and dissection of new enzyme activities.

1407 related Products with: Interrogation of Benzomalvin Biosynthesis Using Fungal Artificial Chromosomes with Metabolomic Scoring (FAC-MS): Discovery of a Benzodiazepine Synthase Activity.

Rapid Microplate Assay K Acyl CoA Synthase Benzodiazepine antibody, Benzodiazepine antibody, Ampliteâ„¢ Universal Fluo Ampliteâ„¢ Universal Fluo Ampliteâ„¢ Universal Fluo Ampliteâ„¢ Universal Fluo Ampliteâ„¢ MMP 3 Activity Ampliteâ„¢ Fluorimetric H MS-275 (Entinostat, SNDX- RANK Ligand Soluble, Huma

Related Pathways

#29514855   // Save this To Up

The Novel C-terminal Truncated 90-kDa Isoform of Topoisomerase II (TOP2/90) Is a Determinant of Etoposide Resistance in K562 Leukemia Cells via Heterodimerization with the TOP2/170 Isoform.

DNA topoisomerase II (170 kDa, TOP2/170) is essential in proliferating cells by resolving DNA topological entanglements during chromosome condensation, replication, and segregation. We previously characterized a C-terminally truncated isoform (TOP2/90), detectable in human leukemia K562 cells but more abundantly expressed in a clonal subline, K/VP.5, with acquired resistance to the anticancer agent etoposide. TOP2/90 (786 aa) is the translation product of a TOP2 mRNA that retains a processed intron 19. TOP2/90 lacks the active-site tyrosine-805 required to generate double-strand DNA breaks as well as nuclear localization signals present in the TOP2/170 isoform (1531 aa). Here, we found that TOP2/90, like TOP2/170, was detectable in the nucleus and cytoplasm of K562 and K/VP.5 cells. Coimmunoprecipitation of endogenous TOP2/90 and TOP2/170 demonstrated heterodimerization of these isoforms. Forced expression of TOP2/90 in K562 cells suppressed, whereas siRNA-mediated knockdown of TOP2/90 in K/VP.5 cells enhanced, etoposide-mediated DNA strand breaks compared with similarly treated cells transfected with empty vector or control siRNAs, respectively. In addition, forced expression of TOP2/90 in K562 cells inhibited etoposide cytotoxicity assessed by clonogenic assays. qPCR and immunoassays demonstrated TOP2/90 mRNA and protein expression in normal human tissues/cells and in leukemia cells from patients. Together, results strongly suggest that TOP2/90 expression decreases drug-induced TOP2-DNA covalent complexes and is a determinant of chemoresistance through a dominant-negative effect related to heterodimerization with TOP2/170. Alternative processing of TOP2 pre-mRNA, and subsequent synthesis of TOP2/90, may be an important mechanism regulating the formation and/or stability of cytotoxic TOP2/170-DNA covalent complexes in response to TOP2-targeting agents.

1687 related Products with: The Novel C-terminal Truncated 90-kDa Isoform of Topoisomerase II (TOP2/90) Is a Determinant of Etoposide Resistance in K562 Leukemia Cells via Heterodimerization with the TOP2/170 Isoform.

FDA Standard Frozen Tissu FDA Standard Frozen Tissu Goat Anti-Human Laforin ( interleukin 17 receptor C V-ATPase 116 kDa isoform Goat Anti-Human MBD2 (iso Goat Anti-Human MDM2 (iso Goat Anti-Human NHERF2 (i Goat Anti-Human Nur77 TR3 Goat Anti-Human NHERF2 (i Goat Anti-Human SLIMMER F Goat Anti- TRIM5 RNF88 (a

Related Pathways

#29475994   // Save this To Up

Chromosome Cohesion and Condensation in Egg Extracts.

Chromosome structure in both interphase and M-phase cells is strongly influenced by the action of the cohesin and condensin protein complexes. The cohesin complex tethers the identical copies of each chromosome, called sister chromatids, together following DNA replication and promotes normal interphase chromosome structure and gene expression. In contrast, condensin is active largely in M phase and promotes the compaction of individual chromosomes. The egg extract system is uniquely suited to analyze the functions of both complexes. Egg extracts, in which the cell cycle state can be manipulated, contain stockpiles of nuclear proteins (including condensin and cohesin) sufficient for the assembly of thousands of nuclei per microliter. Extract prepared from unfertilized eggs is arrested by the presence of cytostatic factor (CSF) in a state with high levels of M-phase kinase activity, but can be stimulated to enter interphase, in which DNA replication occurs spontaneously. For cohesion assays, demembranated sperm nuclei are incubated in interphase extract, where they undergo rapid and synchronous DNA replication and cohesion establishment through the recruitment of proteins and other factors (e.g., nucleotides) from the extract. Sister chromatid cohesion is assessed by then driving the extract into M phase by the addition of fresh CSF-arrested extract. In contrast, because chromosome condensation occurs spontaneously in M-phase extracts, sperm nuclei are added directly to CSF extracts to assay condensation.

1050 related Products with: Chromosome Cohesion and Condensation in Egg Extracts.

DNA (cytosine 5) methyltr Anti-ACIN1ACIN1(Apoptotic Anti ACIN1ACIN1(Apoptotic Interleukin-34 IL34 (N-t Interleukin-34 IL34 anti Sterile filtered goat se Sterile filtered goat se Sterile filtered mouse s Sterile filtered rat ser ING1B antisense ING1B sense Interferon γ

Related Pathways