Sentences with phrase «cohesin in»

Stage - specific binding profiles of cohesin in resting and activated B lymphocytes suggest a role for cohesin in immunoglobulin class switching and maturation.

Gamze Gunal (Jessberger, TUD)-- «Stage - specific binding profile of cohesin in resting and switch - activated B lymphocytes» (2013)

Not exact matches

Mutations in the genes encoding proteins that regulate cohesin and cohesin protein itself cause the developmental disorder Cornelia de Lange syndrome (CdLS).

«This also raises the possibility that mild mutations in cohesin genes may be the cause of some fraction of congenital heart defects in the general population,» she says.

Research coordinated by Osaka University has now shown that the nuclear protein complex cohesin must be expressed at sufficient levels in the early mouse brain to control gene regulation and allow development of healthy neuronal networks and behavioral characteristics.

«Now, through our new study, we show that lowering levels of a particular cohesin protein called Rad21 in embryonic zebrafish produces similar types of heart defects to those found in people with CdLS,» Associate Professor Horsfield says.

CdLS is known to result from mutations in subunits or regulators of cohesin, a group of linked proteins necessary for cell division and other cell processes.

«We also found that reduced cohesin led to changes in the expression of genes involved in nerve cell development and the response to an immune signaling protein,» corresponding author Toshihide Yamashita says.

Unless sufficient cohesin was present in the developing mouse brain, the researchers showed that the regulation of a number of genes was disrupted, leading to neuronal defects and increased anxiety.

Since the two new DNA strands are caught in the ring, only one cohesin is needed to mark the two, thereby helping the transcription factors to find their original binding region on both DNA strands.

Gabriela Cabral, a PhD student in the lab of Alex Dammermann at the Center for Molecular Biology of the University of Vienna, explains: «Many people thought that centrioles are held together by the same glue as chromosomes, a substance called cohesin, which is destroyed during cell division.

Cohesins are protein complexes that bind two straps of DNA and are implicated in its repair, replication and recombination, as well as in its chromosomal stability, transcription regulation, stem - cell pluripotency, and cell differentiation.

In previous studies, researchers proved in mice that genes of the meiotic cohesin complex produce various degrees of infertility in micIn previous studies, researchers proved in mice that genes of the meiotic cohesin complex produce various degrees of infertility in micin mice that genes of the meiotic cohesin complex produce various degrees of infertility in micin mice.

CSIC researcher adds: «We have confirmed that mutation is found in both copies of the gene, one inherited from the father and the other one inherited from the mother, in the four women affected by the disease, causing an absolute absence of STAG3 protein and meiotic cohesin complex in these women.

His research currently focuses on determining the mechanisms and consequences of cohesin gene inactivation in human cancer.

«By knowing which of the Cohesin / CTCF bound sites are coming together in physical proximity, we started to go from a linear view of the genome to sets of looping interactions, which led us to these domains, these super enhancer domains, where gene expression enhancement is contained within the loop,» says Jill Dowen, a postdoctoral researcher in Young's lab.

In the ESCs they studied, the scientists identified 197 Cohesin / CTCF - flanked loops that contain active genes and enhancers, and 349 loops that contain repressed genes.

Hnisz, also a postdoctoral researcher in Young's lab, likens the loops to «goody bags», with Cohesin and CTCF acting as the purse strings to create a DNA loop that cradles proteins enhancing or repressing gene expression.

Interestingly, when mouse neural precursor cells were examined for similar Cohesin / CTCF - bound loops, not only did the cells have such loops, but they were in similar locations as in the ESC genome.

According to our current understanding, cohesin is already loaded onto DNA (along the entire length of the decondensed one - chromatid chromosome) in telophase, i.e. only minutes after chromosome segregation, by opening / closing its Smc1 - Smc3 interaction site (or «entry gate»).

That poses an obvious problem during S phase: While DNA replication machineries («replisomes») zip along the chromosomes trying to faithfully duplicate the entire genome in a matter of just a couple of hours, they encounter — on average — multiple cohesin rings that are already wrapped around DNA.

Cohesin obviously gets its name from the fact that it causes «cohesion» between sister chromatids, which has been first described 20 years ago in budding yeast.

Cohesin has also been shown to have functions in transcriptional regulation.

However, a small but very important fraction of cohesin molecules, which is located at the chromosomes» centromere regions, remains protected from this removal mechanism in prophase.

It is important to mention that cohesin also has a very unique role in meiosis where it not only coheses sister chromatids but also chromosomal homologs (the two maternal / paternal versions of a chromosome, each consisting of two sisters, which themselves are cohesed).

The last stage in the life of a cohesin ring is its removal from centromeres, a tightly regulated process, which involves proteolytic cleavage of cohesin's Scc1 / Rad21 subunit (see Figure 2).

Since actual cohesion defects will cause mitotic failure (which most surely results in cell death), most of cohesin - associated diseases are believed to be caused by misregulation of the complex's non-canonical functions in replication / transcription.

Because of its pleiotropic functions, defects in human cohesin biology can cause a number of clinically relevant issues.

More specifically, we have been studying the roles of the condensin and cohesin complexes in 3D genome organization in the fission yeast, mouse and human systems.

After twenty years of research, the cohesin complex still manages to surprise us regularly, as new functions in new areas of cell cycle regulation come to light.

Currently, extensive research is conducted to better understand the role of certain cohesin mutations in cancers such as glioblastoma, or Ewing's sarcoma.

By combining the fission yeast, mouse, and human systems with the latest genomic, genetic, cell biological, and biochemical approaches, we seek to determine how condensin and cohesin organize the functional 3D genome structures and participate in various biological processes, including transcriptional regulation and chromosomal dynamics, and how they contribute to oncogenic processes.

These studies demonstrate that the two important protein complexes, condensin and cohesin, are both essential for the assembly of the functional genome architecture, but their roles in the 3D genome organization (gene contacts and topological domain organization) are significantly different.

In the figure: ChIA - PET genomic analyses successfully mapped condensin (left) and cohesin (right)- mediated gene contacts throughout the fission yeast genome.