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PMID: 15192699 Published · ppublish English Journal Article

Histone variant H2ABbd confers lower stability to the nucleosome.

EMBO reports ·Vol. 5 ·No. 7 ·2004-07-00 ·Pages 715-20

Gautier T, Abbott DW, Molla A, Verdel A, Ausio J, Dimitrov S

Abstract

The histone H2ABbd is a novel histone variant of H2A with a totally unknown function. We have investigated the behaviour of the H2ABbd nucleosomes. Nucleosomes were reconstituted with recombinant histone H2ABbd and changes in their conformations at different salt concentrations were studied by analytical centrifugation. The data are in agreement with H2ABbd being less tightly bound compared with conventional H2A in the nucleosome. In addition, stable cell lines expressing either green fluorescent protein (GFP)-H2A or GFP-H2ABbd were established and the mobility of both fusions was measured by fluorescence recovery after photobleaching. We show that GFP-H2ABbd exchanges much more rapidly than GFP-H2A within the nucleosome. The reported data are compatible with a lower stability of the variant H2ABbd nucleosome compared with the conventional H2A particle.

MeSH Terms
Animals Centrifugation Chickens Dose-Response Relationship, Drug Erythrocytes/metabolism Green Fluorescent Proteins/metabolism Histones/chemistry,metabolism,physiology Immunoblotting Microscopy, Fluorescence Nucleosomes/metabolism Recombinant Fusion Proteins/metabolism Sodium Chloride/pharmacology Time Factors Transfection Ultracentrifugation
Chemicals
Histones Nucleosomes Recombinant Fusion Proteins Green Fluorescent Proteins Sodium Chloride
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Gautier Thierry
Institut Albert Bonniot, INSERM U309, 38706 La Tronche cedex, France.
Abbott D Wade
Molla Annie
Verdel Andre
Ausio Juan
Dimitrov Stefan
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Article Info
Journal
EMBO reports
Abbr.
EMBO Rep
ISSN
1469-221X
Published
2004-07-00
Epub
2004-00-11
Pages
715-20
Language
English
Region
England
NLM ID
100963049
PMCID
PMC1299093
Subset
IM
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