Histone acetylation in Zea mays. II. Biological significance of post-translational histone acetylation during embryo germination.
Multiple forms of histone acetyltransferases and histone deacetylases, which have been separated and characterized in the accompanying manuscript (López-Rodas, G., Georgieva, E. I., Sendra, R., and Loidl, P. (1991) J. Biol. Chem. 266, 18745-18750), together with in vivo acetate incorporation, were studied during the germination of Zea mays embryos. Total histone acetyltransferase activity increases during germination with two maxima at 40 and 72 h after start of germination. This fluctuation is mainly due to the cytoplasmic B-enzyme which predominantly acetylates histone H4 up to the diacetylated form. The nuclear histone acetyltransferase A2, specific for H3, is low throughout germination, except at 24 h, when it transiently becomes the main activity. Both enzymes are also present in the dry embryo, whereas the second nuclear enzyme A1, specific for H3 and H4, is absent in the initial stage of differentiation. The two histone deacetylases, HD1 and HD2, exhibit entirely different patterns. Whereas HD1 activity is low in the dry embryo and increases during germination, HD2 is the predominant enzyme at the start of differentiation, but almost disappears at later stages. Analysis of the in vivo acetate incorporation reveals that H4 is present in up to tetraacetylated subspecies. The pattern of acetate incorporation into core histones closely resembles the fluctuations of histone acetyltransferase B. Based on the analysis of thymidine kinase activity a close correlation was established between histone acetyltransferase B and DNA replication, whereas the A2 enzyme is associated with transcriptional activity. Histone deacetylase HD1 obviously serves a specific function in the dry embryo and could be a prerequisite for DNA repair processes. The study confirms the idea of DNA repair processes. The study confirms the idea of multiple functions of histone acetylation and assigns distinct enzymes, involved in this modification, to certain nuclear processes.
Department of Microbiology, University of Innsbruck, Medical School, Austria.
E I
EI
Georgieva
G
G
López-Rodas
R
R
Sendra
P
P
Gröbner
P
P
Loidl
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism*; D000818:Animals; D002454:Cell Differentiation; D002645:Chickens; D051548:Histone Acetyltransferases; D006655:Histone Deacetylases / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D010940:Plant Proteins / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity; D003313:Zea mays / Q000196:embryology / Q000201:enzymology*
D006657:Histones; D046911:Macromolecular Substances; D010940:Plant Proteins; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D006655:Histone Deacetylases