SUMO association with repressor complexes, emerging routes for transcriptional control.

@article{GarcaDomnguez2009SUMOAW,
  title={SUMO association with repressor complexes, emerging routes for transcriptional control.},
  author={Mario Garc{\'i}a-Dom{\'i}nguez and Jos{\'e} C. Reyes},
  journal={Biochimica et biophysica acta},
  year={2009},
  volume={1789 6-8},
  pages={
          451-9
        }
}
Characterizing the Role of SUMO in Transcriptional Repression in S. cerevisiae
TLDR
The SSR was characterized following a variety of stresses and time courses and mutants and inhibitors were used to demonstrate that the SSR is triggered by coordinated transcriptional changes (such as in response to a stress).
Control of nuclear activities by substrate-selective and protein-group SUMOylation.
TLDR
It is proposed that collective SUMOylation is typical for nuclear assemblies and argued that SUMO serves as a distinguishing mark for functionally engaged protein fractions.
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New conceptual frameworks suggested by these fi ndings have motivated the development of new methodologies to study preand post-SUMOylation events in vitro and in vivo, using distinct model organisms.
Sumoylation of transcription factor Gcn4 facilitates its Srb10-mediated clearance from promoters in yeast.
TLDR
This study demonstrates an unexpected role for protein sumoylation in the process of transcriptional activation, and shows that clearance of sumoylated Gcn4 requires the protein kinase and Mediator complex subunit Srb10, linking activator removal with target gene transcription.
Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins
TLDR
One story that is beginning to unfold is that SUMO may regulate the microtubule motor protein dynein by modification of its adaptor Lis1 and other possible functions for cytoskeletal sumoylation are also discussed.
SUMO functions in constitutive transcription and during activation of inducible genes in yeast.
TLDR
These findings establish unexpected roles for sumoylation in both constitutive and activated transcription, and provide a novel mechanism for regulating gene expression.
Chromatin modification by SUMO-1 stimulates the promoters of translation machinery genes
TLDR
The occupancy of Small Ubiquitin-like MOdifier (SUMO)-1 on chromatin in HeLa cells is determined by use of chromatin affinity purification coupled with next-generation sequencing to support the concept that the marking of promoters by SUMO-1 is associated with transcriptional activation of genes involved in ribosome biosynthesis and in the protein translation process.
The Regulation of Chromatin by Dynamic SUMO Modifications.
TLDR
These newly appreciated patterns of genome-wide sumoylation will inform more directed studies aimed at analyzing how the dynamics of gene expression are controlled by posttranslational SUMO modification.
Mechanisms of the intracellular localization of the SUMO-activating enzyme Aos1/Uba2
TLDR
The presented work aimed to identify the mechanisms underlying the intracellular localization of the SUMO E1 complex and suggest that thioester charged Ubc9 may shuttle to and allow efficient SUMOylation both in the nuclear and cytoplasmic compartment.
Identification of a Non-covalent Ternary Complex Formed by PIAS1, SUMO1, and UBC9 Proteins Involved in Transcriptional Regulation*
TLDR
The results reveal that UBC9 and PIAS1 are engaged both in a canonical E2·E3 interaction as well as assembled into a previously unidentified non-covalent ternary complex with SUMO as evidenced by bioluminescence resonance energy transfer, nuclear magnetic resonance spectroscopy, and isothermal titration calorimetry studies.
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