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Prothymosin α is a component of a linker histone chaperone
Author(s) -
George Eric M.,
Brown David T.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.04.065
Subject(s) - linker , linker dna , histone , chromatin , microbiology and biotechnology , chaperone (clinical) , chemistry , histone h1 , nucleosome , histone code , biochemistry , chromatosome , biology , biophysics , dna , medicine , pathology , computer science , operating system
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 α (ProTα) can facilitate H1 displacement from and deposition onto the native chromatin template. Depletion of ProTα 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 ProTα is a component of a linker histone chaperone.