Results 11 to 20 of about 3,623 (177)
Different NIPBL requirements of cohesin-STAG1 and cohesin-STAG2
Nature Communications, 2022 Abstract Cohesin organizes the genome through the formation of chromatin loops. NIPBL activates cohesin’s ATPase and is essential for loop extrusion, but its requirement for cohesin loading is currently unclear. Here we have examined the effect of reducing NIPBL levels on the behavior of the two cohesin variants carrying STAG1 or STAG2 ...
Dácil Alonso Gil +4 more
openaire +4 more sources
The Journal of Reproduction and Development, 2023 RAD2lL and REC8, meiosis-specific paralogs of the canonical cohesin subunit RAD21, are essential for proper formation of axial/lateral elements of the synaptonemal complex, synapsis of homologous chromosomes, and crossover recombination in mammalian ...
Yuto TANIUCHI +7 more
doaj +1 more source
Cohesins and Cohesin-Regulators in Meiosis [PDF]
, 2012 Cells have rigorous mechanisms controlling sister chromatid cohesion during cell division to ensure proper distribution of genetic material to daughter cells. Errors in these mechanisms often lead to aneuploidy, frequently implicated in cell death, tumour development and infertility.
Adela Calvente, Jos L.
openaire +1 more source
The torments of the cohesin ring [PDF]
Nucleus, 2017 Cohesin is a ring-shaped protein complex which comprises the Smc1, Smc3 and Scc1 subunits. It topologically embraces chromosomal DNA to connect sister chromatids and stabilize chromatin loops. It is required for proper chromosomal segregation, DNA repair and transcriptional regulation. We have recently reported that cohesin rings can adopt a "collapsed"
Chavda, A., Ang, K., Ivanov, D.
openaire +3 more sources
Cohesin and chromosome segregation [PDF]
Current Biology, 2018 Cohesin is a ring-shaped protein complex that organises the genome, enabling its condensation, expression, repair and transmission. Cohesin is best known for its role in chromosome segregation, where it provides the cohesion that is established between the two newly duplicated sister chromatids during S phase.
Makrantoni, Vasso, Marston, Adele L
openaire +2 more sources
Cohesin and Human Disease [PDF]
Annual Review of Genomics and Human Genetics, 2008 Cornelia de Lange syndrome (CdLS) is a dominant multisystem disorder caused by a disruption of cohesin function. The cohesin ring complex is composed of four protein subunits and more than 25 additional proteins involved in its regulation. The discovery that this complex also has a fundamental role in long-range regulation of transcription in ...
Jinglan, Liu, Ian D, Krantz
openaire +2 more sources
Cohesin Mutations in Cancer [PDF]
Cold Spring Harbor Perspectives in Medicine, 2016 Cohesin is a large ring-shaped protein complex, conserved from yeast to human, which participates in most DNA transactions that take place in the nucleus. It mediates sister chromatid cohesion, which is essential for chromosome segregation and homologous recombination (HR)-mediated DNA repair.
Magali, De Koninck, Ana, Losada
openaire +2 more sources
Dependency of Heterochromatin Domains on Replication Factors
G3: Genes, Genomes, Genetics, 2018 Chromatin structure regulates both genome expression and dynamics in eukaryotes, where large heterochromatic regions are epigenetically silenced through the methylation of histone H3K9, histone deacetylation, and the assembly of repressive complexes ...
Leonie Johanna Jahn +5 more
doaj +1 more source
Pds5 promotes cohesin acetylation and stable cohesin–chromosome interaction [PDF]
The EMBO Reports, 2012 Pds5 and Wpl1 act as anti-establishment factors preventing sister-chromatid cohesion until counteracted in S-phase by the cohesin acetyl-transferase Eso1. However, Pds5 is also required to maintain sister-chromatid cohesion in G2. Here, we show that Pds5 is essential for cohesin acetylation by Eso1 and ensures the maintenance of cohesion by promoting a
Vaur, Sabine +4 more
openaire +4 more sources
eLife, 2021 DNA loops can be formed by a mechanism in which the cohesin complex pulls DNA strands through its ring structure using biased Brownian motion.
Kazuhiro Maeshima, Shiori Iida
openaire +3 more sources