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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Specificity of Zea mays histone deacetylase is regulated by phosphorylation.

Mono Q ion exchange high performance liquid chromatography (HPLC) reveals that the main histone deacetylase activity ( HD1) of germinating Zea mays embryos consists of multiple enzyme forms. Chromatography of HD1 after treatment with alkaline phosphatase yields two distinct histone deacetylase forms (HD1-A, HD1-B). The same is true for chromatography after phosphatase treatment of a total cell extract. One of these enzyme forms (HD1-A) is subject to phosphorylation, which causes a change in the substrate specificity of the enzyme, as shown with HPLC-purified individual core histone species; the substrate specificity for H2A increases more than 2-fold after phosphorylation, whereas the specificity for H3 decreases to about 60%. The total histone deacetylase activity is quantitatively released from isolated nuclei after extraction with moderate ionic strength buffers; no significant residual enzyme activity could be detected in the nuclear matrix.[1]

References

  1. Specificity of Zea mays histone deacetylase is regulated by phosphorylation. Brosch, G., Georgieva, E.I., López-Rodas, G., Lindner, H., Loidl, P. J. Biol. Chem. (1992) [Pubmed]
 
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