Portal de Pesquisa da BVS Veterinária

Anim. Reprod.; 7(3): 204-204, July/September 2010.

Artigo em Inglês | VETINDEX | ID: vti-5919

Resumo

Our laboratory is interested in post-translational modifications of histone proteins, with studies ranging from identification of novel modifications to functional characterization of these marks. Ultimately, we seek to provide a greater understanding of how histone modifications work together to form a ‘histone code. This code is thought to regulate the recruitment of effector proteins that regulate the diverse functions associated with DNA, including gene transcription and DNA repair. Our recent studies show that RNA polymerase II recruits a variety of chromatin modifying enzymes that contribute to the disruption, reassembly and maintenance of chromatin structure during the transcription elongation process. One enzyme we have focused on is Set2, which associates with the transcribing polymerase and methylates nucleosomal H3 on lysine 36. H3K36 methylation results in the recruitment of a histone deacetylase complex which functions to prevent inappropriate transcription initiation from occurring within the transcribed regions of genes. I will discuss our recent progress toward understanding how Set2 contributes to the organization and function of chromatin. In addition, I will highlight our progress on a proteomics project that is providing new insights into how “readers” of the histone code bind their cognate modifications using high-density histone peptide arrays.(AU)

Biblioteca responsável: BR68.1

Localização: BR68.1