Analysis Biomolecular Interactions of Protein with Histone Peptides by BLI (CAT#: STEM-MB-0092-CJ)

Introduction

Eukaryotic chromatin structure is broadly divided into euchromatin and heterochromatin, with heterochromatin structure further subdivided depending on the combination of histone post-translational modifications (PTMs). These PTMs alter not only the chromatin conformation but also establish direct regulatory roles in gene expression and protein recruitment. Myriad combinations of histone PTMs–including acetylation, phosphorylation, methylation, ubiquitination, biotinylation, sumoylation, and proline isomerization, collectively known as the“histone marks”–can be found, particularly on the unstructured N-terminal tail protruding from the nucleosomal core. These PTMs can regulate numerous cellular processes, including gene transcription, cell division, and DNA damage repair, through the activities of different “readers” or effector proteins.