Anti-Ubiquitin+1 polyclonal antibody (DPAB2686)


Host Species
Antibody Isotype
Species Reactivity
Synthetic peptide


Alternative Names
Ubiquitin+1; Ub+1; FLJ25987; MGC8385; Polyubiquitin B; RPS27A


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Meiotic Double-Strand Break Processing and Crossover Patterning Are Regulated in a Sex-Specific Manner by BRCA1-BARD1 in Caenorhabditis elegans


Authors: Li, Qianyan; Hariri, Sara; Engebrecht, JoAnne

Meiosis is regulated in a sex-specific manner to produce two distinct gametes, sperm and oocytes, for sexual reproduction. To determine how meiotic recombination is regulated in spermatogenesis, we analyzed the meiotic phenotypes of mutants in the tumor suppressor E3 ubiquitin ligase-complex inCaenorhabditis elegansmale meiosis. Unlike in mammals, this complex is not required for meiotic sex chromosome inactivation, the process whereby hemizygous sex chromosomes are transcriptionally silenced. Interestingly,andmutants show meiotic recombination phenotypes that are largely opposing to those previously reported for female meiosis. Fewer meiotic recombination intermediates marked by the recombinasewere observed inandmutants, and the reduction infoci could be suppressed by mutation of nonhomologous-end-joining proteins. Analysis of GFP::RPA-1 revealed fewer foci in themutant and concentration of-to sites of meiotic recombination was dependent on DNA end resection, suggesting that the complex regulates the processing of meiotic double-strand breaks to promote repair by homologous recombination. Further,-is important to promote progeny viability when male meiosis is perturbed by mutations that block the pairing and synapsis of different chromosome pairs, although the complex is not required to stabilize thefilament as in female meiosis under the same conditions. Analyses of crossover designation and formation revealed that-inhibits supernumerary COs when meiosis is perturbed. Together, our findings suggest that-regulates different aspects of meiotic recombination in male and female meiosis.

Early but not late conformational changes of tau in association with ubiquitination of neurofibrillary pathology in Alzheimer's disease brains


Authors: Ibarra-Bracamontes, Vanessa J.; Escobar-Herrera, Jaime; Kristofikova, Zdena; Ripova, Daniela; Floran-Garduno, Benjamin; Garcia-Sierra, Francisco

In Alzheimer's disease, tau protein undergoes post-translational modifications including hyperphosphorylation and truncation, which promotes two major conformational changes associated with progressive N-terminal folding. Along with the development of the disease, tau ubiquitination was previously shown to emerge in the early and intermediate stages of the disease, which is closely associated with early tau truncation at aspartic acid 421, but not with a subsequently truncated tau molecule at glutamic acid 391. In the same group of cases, using multiple immunolabeling and confocal microscopy, a possible relationship between the ubiquitin-targeting of tau and the progression of conformational changes adopted by the N-terminus of this molecule was further studied. A comparable number of neurofibrillary tangles was found displaying ubiquitin, an early conformation recognized by the Alz-50 antibody, and a phosphorylation. However, a more reduced number of neurofibrillary tangles were immunoreactive to Tau-66 antibody, a late tau conformational change marker. When double-labeling profiles of neurofibrillary tangles were assessed, ubiquitination was clearly demonstrated in tau molecules undergoing early N-terminal folding, but was barely observed in late conformational changes of the N-terminus adopted by tau. The same pattern of colocalization was visualized in neuritic pathology. Overall, these results indicate that a more intact conformation of the N-terminus of tau may facilitate tau ubiquitination, but this modification may not occur in a late truncated and more compressed folding of the N-terminus of the tau molecule.

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