Protein ubiquitination is one of the most powerful posttranslational modifications of proteins,
as it regulates a plethora of cellular processes in distinct manners. Simple …

Nucleosomes are efficient DNA-packaging units. The fundamental protein unit of the
nucleosome is the histone dimer, a simple α-helical domain possessing a highly basic …

Deubiquitinating enzymes (DUBs) are proteases that process ubiquitin or ubiquitin-like gene
products, reverse the modification of proteins by a single ubiquitin (-like) protein, and …

Covalent modifications of histone tails have fundamental roles in chromatin structure and
function. One such modification, lysine methylation, has important functions in many …

Ubiquitination is a reversible posttranslational modification of cellular proteins, in which a 76–
amino acid polypeptide, ubiquitin, is primarily attached to the ϵ-amino group of lysines in …

Over the past 10 years, the study of histone acetyltransferases (HATs) has advanced
significantly, and a number of HATs have been isolated from various organisms. It emerged …

Attachment of ubiquitin to proteins is a crucial step in many cellular regulatory mechanisms
and contributes to numerous biological processes, including embryonic development, the …

In eukaryotes, the core promoter serves as a platform for the assembly of transcription
preinitiation complex (PIC) that includes TFIIA, TFIIB, TFIID, TFIIE, TFIIF, TFIIH, and RNA …

Gene transcription by RNA polymerase II is regulated by activator proteins that recruit the
coactivator complexes SAGA (Spt–Ada–Gcn5–acetyltransferase), and transcription factor IID …

It is more evident now than ever that nucleosomes can transmit epigenetic information from
one cell generation to the next. It has been demonstrated during the past decade that the …