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 chromatinmodifying 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.
Assuntos
Animais , Bovinos , Polimorfismo Genético/genética , RNA Nuclear Pequeno/análise , Expressão Gênica/genéticaResumo
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 chromatinmodifying 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)
Assuntos
Animais , Bovinos , Polimorfismo Genético/genética , RNA Nuclear Pequeno/análise , Expressão Gênica/genéticaResumo
No presente estudo, estimou-se a abundância dos transcritos da miostatina foi estimada durante a embriogênese de galinha por análises de RT-PCR competitiva. Níveis basais de mRNA desse gene foram detectados até o estádio HH15, enquanto acúmulos significativos nesses níveis foram observados apenas no estádio HH24, seguido por redução na abundância desses transcritos a partir do estádio HH26. Tais descobertas preliminares proporcionam informações relevantes sobre a ativação do fator de crescimento miostatina durante o desenvolvimento in ovo de aves.(AU)