[PDF][PDF] Nuclear genome organization in fungi: From gene folding to Rabl chromosomes
DE Torres, AT Reckard, AD Klocko… - FEMS Microbiology …, 2023 - academic.oup.com
Comparative genomics has recently provided unprecedented insights into the biology and
evolution of the fungal lineage. In the postgenomics era, a major research interest focuses …
evolution of the fungal lineage. In the postgenomics era, a major research interest focuses …
Nuclear envelope, chromatin organizers, histones, and DNA: The many achilles heels exploited across cancers
AK Balaji, S Saha, S Deshpande, D Poola… - Frontiers in Cell and …, 2022 - frontiersin.org
In eukaryotic cells, the genome is organized in the form of chromatin composed of DNA and
histones that organize and regulate gene expression. The dysregulation of chromatin …
histones that organize and regulate gene expression. The dysregulation of chromatin …
LEM2 phase separation promotes ESCRT-mediated nuclear envelope reformation
During cell division, remodelling of the nuclear envelope enables chromosome segregation
by the mitotic spindle. The reformation of sealed nuclei requires ESCRTs (endosomal …
by the mitotic spindle. The reformation of sealed nuclei requires ESCRTs (endosomal …
[HTML][HTML] Positioning heterochromatin at the nuclear periphery suppresses histone turnover to promote epigenetic inheritance
In eukaryotes, heterochromatin is generally located at the nuclear periphery. This study
investigates the biological significance of perinuclear positioning for heterochromatin …
investigates the biological significance of perinuclear positioning for heterochromatin …
Establishment of centromere identity is dependent on nuclear spatial organization
W Wu, T McHugh, DA Kelly, AL Pidoux, RC Allshire - Current Biology, 2022 - cell.com
The establishment of centromere-specific CENP-A chromatin is influenced by epigenetic
and genetic processes. Central domain sequences from fission yeast centromeres are …
and genetic processes. Central domain sequences from fission yeast centromeres are …
Quantitative analysis of nuclear pore complex organization in Schizosaccharomyces pombe
JM Varberg, JR Unruh, AJ Bestul… - Life science …, 2022 - life-science-alliance.org
The number, distribution, and composition of nuclear pore complexes (NPCs) in the nuclear
envelope varies between cell types and changes during cellular differentiation and in …
envelope varies between cell types and changes during cellular differentiation and in …
The SUN-family protein Sad1 mediates heterochromatin spatial organization through interaction with histone H2A-H2B
Heterochromatin is generally associated with the nuclear periphery, but how the spatial
organization of heterochromatin is regulated to ensure epigenetic silencing remains unclear …
organization of heterochromatin is regulated to ensure epigenetic silencing remains unclear …
Nuclear envelope attachment of telomeres limits TERRA and telomeric rearrangements in quiescent fission yeast cells
L Maestroni, C Reyes, M Vaurs, Y Gachet… - Nucleic Acids …, 2020 - academic.oup.com
Telomere anchoring to nuclear envelope (NE) is a key feature of nuclear genome
architecture. Peripheral localization of telomeres is important for chromatin silencing …
architecture. Peripheral localization of telomeres is important for chromatin silencing …
Nuclear envelope proteins modulating the heterochromatin formation and functions in fission yeast
The nuclear envelope (NE) consists of the inner and outer nuclear membranes (INM and
ONM), and the nuclear pore complex (NPC), which penetrates the double membrane. ONM …
ONM), and the nuclear pore complex (NPC), which penetrates the double membrane. ONM …
SUMOylation regulates Lem2 function in centromere clustering and silencing
J Strachan, O Leidecker, C Spanos… - Journal of Cell …, 2023 - journals.biologists.com
Regulation by the small modifier SUMO is heavily dependent on spatial control of enzymes
that mediate the attachment and removal of SUMO on substrate proteins. Here, we show that …
that mediate the attachment and removal of SUMO on substrate proteins. Here, we show that …