[HTML][HTML] Updated understanding of the protein–DNA recognition code used by C2H2 zinc finger proteins

X Zhang, RM Blumenthal, X Cheng - Current Opinion in Structural Biology, 2024 - Elsevier
Abstract C2H2 zinc-finger (ZF) proteins form the largest family of DNA-binding transcription
factors coded by mammalian genomes. In a typical DNA-binding ZF module, there are …

[HTML][HTML] C2H2 zinc finger transcription factors associated with hemoglobinopathies

X Zhang, F Xia, X Zhang, RM Blumenthal… - Journal of molecular …, 2023 - Elsevier
In humans, specific aberrations in β-globin results in sickle cell disease and β-thalassemia,
symptoms of which can be ameliorated by increased expression of fetal globin (HbF). Two …

Single-molecule imaging reveals a direct role of CTCF's zinc fingers in SA interaction and cluster-dependent RNA recruitment

J Huber, NL Tanasie, S Zernia… - Nucleic Acids Research, 2024 - academic.oup.com
CTCF is a zinc finger protein associated with transcription regulation that also acts as a
barrier factor for topologically associated domains (TADs) generated by cohesin via loop …

C2H2 proteins: Evolutionary aspects of domain architecture and diversification

AN Bonchuk, PG Georgiev - BioEssays, 2024 - Wiley Online Library
The largest group of transcription factors in higher eukaryotes are C2H2 proteins, which
contain C2H2‐type zinc finger domains that specifically bind to DNA. Few well‐studied …

[HTML][HTML] Keep Fingers on the CpG Islands

X Zhang, RM Blumenthal, X Cheng - Epigenomes, 2024 - mdpi.com
The post-genomic era has ushered in the extensive application of epigenetic editing tools,
allowing for precise alterations of gene expression. The use of reprogrammable editors that …

A negatively-charged region within carboxy-terminal domain maintains proper CTCF DNA binding

L Liu, Y Tang, Q Wu - bioRxiv, 2024 - biorxiv.org
As an essential regulator of higher-order chromatin structures, CTCF is a highly-conserved
DNA binding protein with a central DNA-binding domain of 11 tandem zinc fingers, which …

Acetylation of H3K115 at the nucleosome dyad is associated with fragile nucleosomes at active regulatory sites.

D Sengupta, ET Friman, RS Illingworth, Y Kumar… - bioRxiv, 2023 - biorxiv.org
Acetylation of lysine residues in the tail domain of histone H3 is well characterized.
However, acetyl-lysines in the histone globular domain also hold regulatory potential …