Prothymosin alpha is a component of a linker histone chaperone.
Linker histone H1 binds with high affinity to naked and nucleosomal DNA in vitro but is rapidly exchanged between chromatin sites in vivo suggesting the involvement of one or more linker histone chaperones. Using permeabilized cells, we demonstrate that the small acidic protein prothymosin alpha (ProTalpha) can facilitate H1 displacement from and deposition onto the native chromatin template. Depletion of ProTalpha levels in vivo by siRNA-mediated mRNA degradation resulted in a decreased rate of exchange of linker histones as assayed by photobleaching techniques. These results indicate that ProTalpha is a component of a linker histone chaperone.
George
Eric M
EM
Department of Biochemistry, University of Mississippi Medical Center, Jackson, MS 39216, USA.
Brown
David T
DT
D000595:Amino Acid Sequence; D000818:Animals; D041702:BALB 3T3 Cells; D002843:Chromatin / Q000235:genetics / Q000378:metabolism*; D036681:Fluorescence Recovery After Photobleaching; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D056488:Histone Chaperones / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D011498:Protein Precursors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D034622:RNA Interference; D013947:Thymosin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D002843:Chromatin; D056488:Histone Chaperones; D011498:Protein Precursors; C040782:prothymosin alpha; D049452:Green Fluorescent Proteins; D013947:Thymosin