The protein Sgf29 has been identified as a subunit of the SAGA (Spt-Ada-Gcn5 acetyltransferase) histone acetyltransferase complex in Saccharomyces cerevisiae, which is conserved from yeast to humans. The tandem tudor domain at the C-terminus of Sgf29 was crystallized using the hanging-drop vapour-diffusion method and the crystals diffracted to 1.92 A resolution. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a=49.76, b=95.10, c=114.43 A, and are estimated to contain one protein molecule per asymmetric unit.
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http://dx.doi.org/10.1107/S1744309110016726 | DOI Listing |
Nat Commun
January 2025
Guangdong Provincial Key Laboratory of Stem Cell and Regenerative Medicine, CAS Key Laboratory of Regenerative Biology, China-New Zealand Joint Laboratory on Biomedicine and Health, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.
UHRF1 maintains DNA methylation by recruiting DNA methyltransferases to chromatin. In mouse, these dynamics are potently antagonized by a natural UHRF1 inhibitory protein STELLA, while the comparable effects of its human ortholog are insufficiently characterized, especially in cancer cells. Herein, we demonstrate that human STELLA (hSTELLA) is inadequate, while mouse STELLA (mSTELLA) is fully proficient in inhibiting the abnormal DNA methylation and oncogenic functions of UHRF1 in human cancer cells.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
August 2024
Hunan Key Laboratory of Molecular Precision Medicine, Department of Neurosurgery, Xiangya Hospital & Center for Medical Genetics, School of Life Sciences, Central South University, Changsha, Hunan, China.
EMBO Rep
September 2024
College of Life Sciences, Hebei University, Baoding, Hebei Province, 071002, China.
The tandem Tudor-like domain-containing protein Spindlin1 (SPIN1) is a transcriptional coactivator with critical functions in embryonic development and emerging roles in cancer. However, the involvement of SPIN1 in DNA damage repair has remained unclear. Our study shows that SPIN1 is recruited to DNA lesions through its N-terminal disordered region that binds to Poly-ADP-ribose (PAR), and facilitates homologous recombination (HR)-mediated DNA damage repair.
View Article and Find Full Text PDFMob DNA
April 2024
Department of Biochemistry, Institute of Biochemistry and Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569, Stuttgart, Germany.
Background: Repeat elements (REs) play important roles for cell function in health and disease. However, RE enrichment analysis in short-read high-throughput sequencing (HTS) data, such as ChIP-seq, is a challenging task.
Results: Here, we present RepEnTools, a software package for genome-wide RE enrichment analysis of ChIP-seq and similar chromatin pulldown experiments.
J Med Chem
October 2023
UNC Eshelman School of Pharmacy, Center for Integrative Chemical Biology and Drug Discovery, Chemical Biology and Medicinal Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States.
Methyl-lysine reader p53 binding protein 1 (53BP1) is a central mediator of DNA break repair and is associated with various human diseases, including cancer. Thus, high-quality 53BP1 chemical probes can aid in further understanding the role of 53BP1 in genome repair pathways. Herein, we utilized focused DNA-encoded library screening to identify the novel hit compound UNC8531, which binds the 53BP1 tandem Tudor domain (TTD) with an IC of 0.
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