Source 1review2001Journal of Biological Chemistry
Toolkit/DRIP/TRAP/Mediator-like coactivator complex
DRIP/TRAP/Mediator-like coactivator complex
Also known as: DRIP, TRAP
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
In to coactivator complexes that nucleosome remodeling or histone acetyltransferase other coactivator complexes have been identified... These factors may function to recruit RNA polymerase II to nuclear receptors.
Usefulness & Problems
Why this is useful
The review describes a coactivator complex class distinct from chromatin remodelers and HAT complexes that may help recruit RNA polymerase II to nuclear receptors. This matches the DRIP/TRAP/Mediator-like theme in the source materials.; linking nuclear receptors to RNA polymerase II recruitment; coactivator function beyond chromatin remodeling and histone acetylation
Source:
The review describes a coactivator complex class distinct from chromatin remodelers and HAT complexes that may help recruit RNA polymerase II to nuclear receptors. This matches the DRIP/TRAP/Mediator-like theme in the source materials.
Source:
linking nuclear receptors to RNA polymerase II recruitment
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coactivator function beyond chromatin remodeling and histone acetylation
Problem solved
It addresses the step of connecting receptor-bound regulatory complexes to the basal transcription machinery. This complements chromatin remodeling and histone acetylation functions.; provides a route for coupling receptor activation to basal transcription machinery
Source:
It addresses the step of connecting receptor-bound regulatory complexes to the basal transcription machinery. This complements chromatin remodeling and histone acetylation functions.
Source:
provides a route for coupling receptor activation to basal transcription machinery
Problem links
provides a route for coupling receptor activation to basal transcription machinery
LiteratureIt addresses the step of connecting receptor-bound regulatory complexes to the basal transcription machinery. This complements chromatin remodeling and histone acetylation functions.
Source:
It addresses the step of connecting receptor-bound regulatory complexes to the basal transcription machinery. This complements chromatin remodeling and histone acetylation functions.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
combinatorial or sequential coactivator action during transcriptional activationligand-dependent corepressor-to-coactivator exchangeprotein complex recruitment of rna polymerase ii/basal transcription machineryTechniques
No technique tags yet.
Target processes
transcriptionImplementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenoperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment
It requires assembly as a multiprotein complex and receptor-dependent recruitment. The abstract does not provide a cleanly preserved subunit list.; acts as part of a large multiprotein coactivator assembly; requires receptor-dependent recruitment context
The abstract does not support a detailed composition map or a full mechanistic comparison with all other coactivator classes. It is therefore less specific than the LXXLL and p160 discussions.; abstract text is partially corrupted and does not cleanly preserve full complex naming or composition; exact mechanistic details are less explicit than for LXXLL or CBP/p300
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
CBP/p300 acetyltransferase activity is described as directly required for enhanced transcription on chromatinized templates.
Ligand-dependent exchange of corepressors for coactivators is presented as the basic mechanism by which nuclear receptors switch from gene repression to activation.
Nuclear receptor transcriptional activation is described as involving multiple factors acting sequentially and/or combinatorially to reorganize chromatin and recruit basal transcription machinery.
p160-family coactivators are described as adapter molecules that recruit CBP and/or p300 complexes to promoter-bound nuclear receptors in a ligand-dependent manner.
Two major coactivator function classes emphasized in the review are ATP-dependent nucleosome remodeling complexes and histone acetyltransferase-containing factors.
The LXXLL motif is described as necessary and sufficient for ligand-dependent interaction with nuclear receptor ligand binding domains, with specificity further influenced by additional residues and ligand-induced receptor conformation.
Approval Evidence
1 source1 linked approval claimfirst-pass slug drip-trap-mediator-like-coactivator-complex
In to coactivator complexes that nucleosome remodeling or histone acetyltransferase other coactivator complexes have been identified... These factors may function to recruit RNA polymerase II to nuclear receptors.
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mechanistic summarysupports
Nuclear receptor transcriptional activation is described as involving multiple factors acting sequentially and/or combinatorially to reorganize chromatin and recruit basal transcription machinery.
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Comparisons
Source-stated alternatives
The review contrasts this class with p160-family adapters, CBP/p300-associated HAT complexes, and SWI/SNF-like remodeling complexes.
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The review contrasts this class with p160-family adapters, CBP/p300-associated HAT complexes, and SWI/SNF-like remodeling complexes.
Source-backed strengths
presented as a distinct coactivator class from remodeling and HAT complexes; suggested to function in RNA polymerase II recruitment
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presented as a distinct coactivator class from remodeling and HAT complexes
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suggested to function in RNA polymerase II recruitment
Compared with CBP/p300 coactivator complex
The review contrasts this class with p160-family adapters, CBP/p300-associated HAT complexes, and SWI/SNF-like remodeling complexes.
Shared frame: source-stated alternative in extracted literature
Strengths here: presented as a distinct coactivator class from remodeling and HAT complexes; suggested to function in RNA polymerase II recruitment.
Relative tradeoffs: abstract text is partially corrupted and does not cleanly preserve full complex naming or composition; exact mechanistic details are less explicit than for LXXLL or CBP/p300.
Source:
The review contrasts this class with p160-family adapters, CBP/p300-associated HAT complexes, and SWI/SNF-like remodeling complexes.
Ranked Citations
- 1.