The Drosophila Nuclear Lamina Protein YA Binds to DNA and Histone H2B with Four Domains
AUTOR(ES)
Yu, Jing
FONTE
The American Society for Cell Biology
RESUMO
Dramatic changes occur in nuclear organization and function during the critical developmental transition from meiosis to mitosis. The Drosophila nuclear lamina protein YA binds to chromatin and is uniquely required for this transition. In this study, we dissected YA's binding to chromatin. We found that YA can bind to chromatin directly and specifically. It binds to DNA but not RNA, with a preference for double-stranded DNA (linear or supercoiled) over single-stranded DNA. It also binds to histone H2B. YA's binding to DNA and histone H2B is mediated by four domains distributed along the length of the YA molecule. A model for YA function at the end of Drosophila female meiosis is proposed.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=65649Documentos Relacionados
- Histone H2A subtypes associate interchangeably in vivo with histone H2B subtypes.
- Mouse histone H2A and H2B genes: four functional genes and a pseudogene undergoing gene conversion with a closely linked functional gene.
- Structure and organization of the chicken H2B histone gene family.
- Histone H2B Ubiquitylation Is Associated with Elongating RNA Polymerase II
- The tail domain of lamin Dm0 binds histones H2A and H2B