Drosophila SIN3 isoforms interact with distinct proteins and have unique biological functions
MM Spain, JA Caruso, A Swaminathan… - Journal of Biological …, 2010 - ASBMB
The SIN3 corepressor serves as a scaffold for the assembly of histone deacetylase (HDAC)
complexes. SIN3 and its associated HDAC have been shown to have critical roles in both …
complexes. SIN3 and its associated HDAC have been shown to have critical roles in both …
Drosophila SIN3 is required at multiple stages of development
SIN3 is a component of a histone deacetylase complex known to be important for
transcription repression. While multiple isoforms of SIN3 have been reported, little is known …
transcription repression. While multiple isoforms of SIN3 have been reported, little is known …
Systematic analysis of SIN3 histone modifying complex components during development
VL Barnes, KA Laity, M Pilecki, LA Pile - Scientific reports, 2018 - nature.com
Establishment and maintenance of histone acetylation levels are critical for metazoan
development and viability. Disruption of the balance between acetylation and deacetylation …
development and viability. Disruption of the balance between acetylation and deacetylation …
Sin3: master scaffold and transcriptional corepressor
Sin3 was isolated over two decades ago as a negative regulator of transcription in budding
yeast. Subsequent research has established the protein as a master transcriptional scaffold …
yeast. Subsequent research has established the protein as a master transcriptional scaffold …
Specific requirement of the chromatin modifier mSin3B in cell cycle exit and cellular differentiation
G David, KB Grandinetti, PM Finnerty… - Proceedings of the …, 2008 - National Acad Sciences
The Sin3-histone deacetylase (HDAC) corepressor complex is conserved from yeast to
humans. Mammals possess two highly related Sin3 proteins, mSin3A and mSin3B, which …
humans. Mammals possess two highly related Sin3 proteins, mSin3A and mSin3B, which …
The SIN3 deacetylase complex represses genes encoding mitochondrial proteins: implications for the regulation of energy metabolism
LA Pile, PT Spellman, RJ Katzenberger… - Journal of Biological …, 2003 - ASBMB
Deacetylation of histones by the SIN3 complex is a major mechanism utilized in eukaryotic
organisms to repress transcription. Presumably, developmental and cellular phenotypes …
organisms to repress transcription. Presumably, developmental and cellular phenotypes …
Sin3: a flexible regulator of global gene expression and genome stability
RA Silverstein, K Ekwall - Current genetics, 2005 - Springer
SIN3 was first identified genetically as a global regulator of transcription. Sin3 is a large
protein composed mainly of protein-interaction domains, whose function is to provide …
protein composed mainly of protein-interaction domains, whose function is to provide …
Co-repressor, co-activator and general transcription factor: the many faces of the Sin3 histone deacetylase (HDAC) complex
GE Adams, A Chandru, SM Cowley - Biochemical Journal, 2018 - portlandpress.com
At face value, the Sin3 histone deacetylase (HDAC) complex appears to be a prototypical co-
repressor complex, that is, a multi-protein complex recruited to chromatin by DNA bound …
repressor complex, that is, a multi-protein complex recruited to chromatin by DNA bound …
Genome-wide studies reveal novel and distinct biological pathways regulated by SIN3 isoforms
Background The multisubunit SIN3 complex is a global transcriptional regulator. In
Drosophila, a single Sin3A gene encodes different isoforms of SIN3, of which SIN3 187 and …
Drosophila, a single Sin3A gene encodes different isoforms of SIN3, of which SIN3 187 and …
Analysis of the chromatin landscape and RNA polymerase II binding at SIN3-regulated genes
I Soukar, A Mitra, LA Pile - Biology Open, 2023 - journals.biologists.com
The chromatin environment has a significant impact on gene expression. Chromatin
structure is highly regulated by histone modifications and RNA polymerase II binding …
structure is highly regulated by histone modifications and RNA polymerase II binding …