@misc{Lawit_Shai_J._Histone_2002,
 author={Lawit, Shai J. and Czarnecka-Verner, Eva},
 volume={58},
 number={3},
 copyright={Creative Commons Attribution BY-SA 4.0 license},
 journal={Biotechnologia, vol.58, 3 (2002)-.},
 howpublished={online},
 year={2002},
 publisher={Committee on Biotechnology PAS},
 publisher={Institute of Bioorganic Chemistry PAS},
 language={eng},
 abstract={Post-translational modifications of histone tails have dramatic ramificationson a variety of vital cellular functions. Removal of the acetyl groups from lysineresidues is catalyzed by histone deacetylases (HDs). Many HDs are known to becomponents of multiprotein complexes such as SIN3 and NuRD that are involved in chromatin condensation and gene regulation. Plants contain a highlyelaborated set of HDs with four distinct classes of these enzymes. Plant HDshave been implicated to play roles in transgene silencing, rDNA regulation,gene expression, and many developmental processes. Seventeen ArabidopsisHDs are apparent in Genbank as are numerous putative HD-interacting partners.Maize HDs have been extensively characterized biochemically, and the use ofpowerful genetic tools currently available in Arabidopsis is rapidly acceleratingthe base of knowledge on the control circuitry of plant chromatin.},
 title={Histone Deacetylase Complexes: Implications for Plants},
 type={Text},
 URL={http://www.rcin.org.pl/Content/137869/PDF/POZN271_172998_biotechnologia-2002-no3-lawit.pdf},
 keywords={biotechnology},
}