Bioinform Adv
Department of Medical Biophysics, University of Toronto, Toronto, ON M5G 1L7, Canada.
Published: March 2023
Summary: Chromatin immunoprecipitation-sequencing is widely used to find transcription factor binding sites, but suffers from various sources of noise. Knocking out the target factor mitigates noise by acting as a negative control. Paired wild-type and knockout (KO) experiments can generate improved motifs but require optimal differential analysis. We introduce peaKO-a computational method to automatically optimize motif analyses with KO controls, which we compare to two other methods. PeaKO often improves elucidation of the target factor and highlights the benefits of KO controls, which far outperform input controls.
Availability And Implementation: PeaKO is freely available at https://peako.hoffmanlab.org.
Contact: michael.hoffman@utoronto.ca.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10074035 | PMC |
http://dx.doi.org/10.1093/bioadv/vbad031 | DOI Listing |
J Neurosurg
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1Department of Neurosurgery, the First Medical Center of Chinese PLA General Hospital, Haidian District, Beijing.
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1Department of Neurosurgery, Medical University of Vienna.
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IMPACT (the Institute for Mental and Physical Health and Clinical Translation), Food & Mood Centre, School of Medicine, Barwon Health, Deakin University, Geelong, Australia.
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Simpson Querrey Institute for Epigenetics and the Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
The testis-specific BET protein BRDT structurally resembles the ubiquitous BRD4 and is misexpressed in cancer, and we show that BRDT misexpression may affect lung cancer progression. BRDT knockdown in lung cancer cells slowed tumor growth and prolonged survival in a xenograft model. Comparative characterization of PTEFb complex participation and chromatin binding indicates BRD4-redundant and BRD4-distinct BRDT functions.
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Department of Biological Chemistry and Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Antigen receptor signaling pathways that control lymphocyte activation depend on signaling hubs and negative regulatory proteins to fine-tune signaling outputs to ensure host defense and avoid pathogenic responses. Caspase recruitment domain-containing protein 11 (CARD11) is a critical signaling scaffold that translates T cell receptor (TCR) triggering into the activation of nuclear factor κB (NF-κB), c-Jun N-terminal kinase (JNK), mechanistic target of rapamycin (mTOR), and Akt. Here, we identify glutamine-rich protein 1 (QRICH1) as a regulator of CARD11 signaling that mediates an intracellular checkpoint for CD8 T cell activation.
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