Histone variant H2ABbd confers lower stability to the nucleosome.
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.
Gautier
Thierry
T
Institut Albert Bonniot, INSERM U309, 38706 La Tronche cedex, France.
Abbott
D Wade
DW
Molla
Annie
A
Verdel
Andre
A
Ausio
Juan
J
Dimitrov
Stefan
S
D000818:Animals; D002498:Centrifugation; D002645:Chickens; D004305:Dose-Response Relationship, Drug; D004912:Erythrocytes / Q000378:metabolism; D049452:Green Fluorescent Proteins / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D015151:Immunoblotting; D008856:Microscopy, Fluorescence; D009707:Nucleosomes / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012965:Sodium Chloride / Q000494:pharmacology; D013997:Time Factors; D014162:Transfection; D014461:Ultracentrifugation
D006657:Histones; D009707:Nucleosomes; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; D012965:Sodium Chloride