In new company: U1 snRNA associates with TAF15

@article{Kugel2009InNC,
  title={In new company: U1 snRNA associates with TAF15},
  author={Jennifer F. Kugel and James A. Goodrich},
  journal={EMBO reports},
  year={2009},
  volume={10}
}
In a recent study published in this issue of EMBO reports, Jobert and colleagues made the unanticipated discovery that a portion of the U1 small-nuclear (sn)RNA in human cells is associated with the transcription factor TAF15 (TATA box-binding protein (TBP)-associated factor 15; Jobert et al, 2009). The U1 snRNA is classically known as a component of the splicing machinery, which removes introns from precursor messenger RNAs (pre-mRNAs). U1 snRNA functions within a protein–RNA complex known as… Expand
Functional insights into the core-TFIIH from a comparative survey.
TLDR
An extended sequence analysis is performed to establish the accurate phylogenetic distribution of the core-TFIIH in 63 eukaryotic organisms and suggest for the first time the implication of the key subunits, P8, P34, P52 and P62 in mRNA splicing via P34. Expand
A comparative genome-wide study of ncRNAs in trypanosomatids
TLDR
This study identified by comparative genomics, and validated by experimental analysis several novel ncRNAs that are conserved across multiple trypanosomatid genomes, and predicted 72 sequences as ncRNA candidates in T. brucei. Expand
α-Amanitin Restrains Cancer Relapse from Drug-Tolerant Cell Subpopulations via TAF15
TLDR
It is consistently found that α-amanitin, an RNA polymerase II (RNAPII) inhibitor, effectively inhibited DTCs by suppressing TAF15 expression, which binds to RNA to modulate transcription and RNA processing. Expand

References

SHOWING 1-10 OF 16 REFERENCES
Human U1 snRNA forms a new chromatin-associated snRNP with TAF15
TLDR
It is shown that a fraction of human U1 snRNA specifically associates with the nuclear RNA‐binding protein TBP‐associated factor 15 (TAF15), suggesting that the U1‐TAF 15 particle is produced by remodelling of the U2‐Sm snRNP. Expand
Crystal structure of human spliceosomal U1 snRNP at 5.5 Å resolution
TLDR
The structure of U1snRNP provides insights into U1 snRNP assembly and suggests a possible mechanism of 5′-splice-site recognition, a hierarchical network of intricate interactions between subunits. Expand
A 69-kD protein that associates reversibly with the Sm core domain of several spliceosomal snRNP species
TLDR
The results are consistent with the working hypothesis that this protein may either play a role in the cytoplasmic assembly of the core domain of the snRNPs and/or in the nuclear transport of thesnRNPs. Expand
U1 snRNA associates with TFIIH and regulates transcriptional initiation
TLDR
The first evidence of the involvement of an snRNA in the regulation of transcriptional initiation is presented, and it is demonstrated that TFIIH, a general transcription initiation factor, specifically associates with U1 snRNA, a core-splicing component. Expand
The spliceosome: the most complex macromolecular machine in the cell?
  • T. Nilsen
  • Biology, Medicine
  • BioEssays : news and reviews in molecular, cellular and developmental biology
  • 2003
TLDR
Technical advances, including new affinity purification methods and improved mass spectrometry techniques, coupled with the completion of many genome sequences, have now permitted a number of proteomic analyses of purified spliceosomes, revealing that thespliceosome is composed of as many as 300 distinct proteins and five RNAs, making it among the most complex macromolecular machines known. Expand
RH70, a Bidirectional RNA Helicase, Co-purifies with U1snRNP*
  • Chee-Gun Lee
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 2002
TLDR
Its association with U1 SnRNP and ATP specificity suggest a role for RH70 in pre-mRNA splicing, in particular, at the early stages of the splicing reaction involving U1snRNP. Expand
The assembly of a spliceosomal small nuclear ribonucleoprotein particle
TLDR
The aim of this review is to briefly outline the structure of snRNPs and to synthesize new and exciting developments in the snRNP biogenesis pathways. Expand
Transcription-dependent colocalization of the U1, U2, U4/U6, and U5 snRNPs in coiled bodies
TLDR
U1 snRNP shows a more widespread nucleoplasmic staining, outside of coiled bodies and "speckled" structures, relative to the other snRNPs, and a novel labeling method is described which shows both the RNA and protein components of individualsnRNPs colocalizing in situ. Expand
Protein Stoichiometry of a Multiprotein Complex, the Human Spliceosomal U1 Small Nuclear Ribonucleoprotein
TLDR
Quantitative mass spectrometry has great potential for the determination of the stoichiometry of multiprotein complexes, and the use of the isotope-coded, amine-specific reagent nicotinoyl-N-oxysuccinimide was found to be advantageous because of its greatermass spectrometric sensitivity. Expand
The DEAD box RNA helicases p68 (Ddx5) and p72 (Ddx17): novel transcriptional co-regulators.
TLDR
The literature demonstrating the action of p68 and, where data are available, p72 as transcriptional co-regulators for a range of transcription factors, namely ERalpha (oestrogen receptor alpha), the tumour suppressor p53, the myogenic regulator MyoD and Runx2, a transcription factor essential for osteoblast development are reviewed. Expand
...
1
2
...