Articles tagged with Histones
Researchers at The Wistar Institute have provided new insights into the emerging theory of gene regulation, showing how two enzymes work together to activate specific genes by loosening chromatin. This study supports the 'histone code' theory, suggesting complex modifications to histones control gene activity.
Scientists discovered protein chromodomains that recognize and bind to specific histone modifications, enabling the regulation of gene expression. This breakthrough could lead to improved treatments for cancer by targeting epigenetic mechanisms.
Researchers have identified two distinct forms of chromatin, a previously unrecognized level of genomic organization. This discovery has broad potential applications in cancer diagnosis and assigning functions to genome subsections.
Researchers at Rockefeller University reveal a crucial link between the Ezh2 protein and chromatin modifications, enabling the development of a wide range of antibodies. The discovery provides new insights into B cell biology and the immune system.
Researchers have linked Polycomb gene silencing to histone protein methylation, explaining the permanence of Hox gene silencing. The study found that Polycomb proteins function through methylating a specific lysine residue on histone 3, leading to permanent gene silencing.
Scientists have identified a unique mechanism used by the Esa1 enzyme to relax DNA packaging, differing from other enzymes in its family. This discovery opens up new possibilities for developing targeted cancer therapies.
Researchers have identified G9a as a chromatin-modifying enzyme essential for normal development. Studies show that G9a deficiency leads to severe developmental growth retardation and increased programmed cell death, highlighting the enzyme's critical role in regulating gene expression during embryogenesis.
Researchers have found a new piece of the gene expression puzzle, revealing how histone proteins interact with each other and with other molecules to regulate gene activity. The discovery sheds light on potential causes of male infertility and highlights the complex mechanisms at play in chromatin.
Using optical tweezers, researchers have observed the dynamic structure of individual nucleosomes for the first time. They found that DNA in these units can be released from histones through a three-stage process, allowing enzymes like RNA polymerase to access genetic information.
A new enzyme called Set2 has been discovered, which regulates gene expression by methylating histone protein H3. This process can help turn genes off, potentially offering a new approach to treating human diseases such as cancer.
Researchers have identified a critical protein, SET7, that regulates gene expression by modifying histone H3. This discovery may lead to new treatments for diseases and provide insights into using stem cells to generate organs. The study reveals that SET7 makes chromatin structure more open, allowing other proteins to access genes.
Researchers at The Wistar Institute have identified a carefully orchestrated series of molecular modifications to p53 that must occur for it to perform its normal function. This discovery may suggest new ways to combat cancers where p53 is dysfunctional, and could also provide insights into the regulation of other DNA-binding proteins.
Research suggests centromeric DNA and histones evolve rapidly, influencing species compatibility. Continuous evolution of centromeric histones may be driving adaptation to changing DNA sequences, contributing to the 'centromere paradox' and species sterility.
Researchers Shiv Grewal and colleagues found that histone H3 variants are linked to gene expression and chromosomal structure. The study suggests a 'histone code' model for organizing the genome into active and silent regions.
A recent Wistar Institute study identifies an enzyme that modifies histones to activate specific genes in yeast. This discovery supports the 'histone code' theory, suggesting a complex interplay among histone modifications controls gene activity.
Scientists have identified a common mode of action among gene-activation molecules linked to cancers, according to a study published in Molecular Cell. The researchers found structural similarities among the molecules, suggesting they may share a unified mechanism of action despite chemical dissimilarities.
Researchers at Memorial Sloan-Kettering Cancer Center have developed a new drug that targets histone deacetylase, an enzyme that regulates cell growth and division. The drug, called SAHA, has shown promise in treating various types of cancer, including breast, lung, and prostate cancers.
Wistar Institute scientists have determined the three-dimensional structure of a key enzyme involved in gene activation, GCN5. The study reveals details on how the enzyme carries out its function and identifies the structural adjustments needed for proper regulation of gene activation.