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PMID: 11854412 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The Drosophila nuclear lamina protein YA binds to DNA and histone H2B with four domains.

Molecular biology of the cell ·Vol. 13 ·No. 2 ·2002-02-00 ·Pages 558-69

Yu J, Wolfner MF

Abstract

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.

MeSH Terms
Animals Chromosomal Proteins, Non-Histone/metabolism Chromosomes/metabolism DNA/metabolism DNA-Binding Proteins/metabolism Drosophila/embryology,metabolism Drosophila Proteins Histones/metabolism Insect Proteins/genetics,metabolism Mitosis/physiology Nuclear Proteins/metabolism Protein Binding Protein Structure, Tertiary
Chemicals
Chromosomal Proteins, Non-Histone DNA-Binding Proteins Drosophila Proteins Histones Insect Proteins Nuclear Proteins fs(1)Ya protein, Drosophila DNA
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Yu Jing
Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853-2703, USA.
Wolfner Mariana F
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
Published
2002-02-00
Pages
558-69
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC65649
Subset
IM
Grants
NIGMS NIH HHS · R01 GM044659 · United States
NIGMS NIH HHS · GM44659 · United States
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