A tale of histone modifications
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Correspondence: Patrick A Grant pag9n@virginia.edu
Genome Biology 2001, 2:reviews0003-reviews0003.6 doi:10.1186/gb-2001-2-4-reviews0003
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Research
L Aravind, Lakshminarayan M Iyer Genome Biology 2002, 3:research0039-research0039.7 (24 July 2002) Using computational sequence-profile analysis methods, a previously uncharacterized, predicted α-helical domain of about 85 residues was identified in chromosomal proteins such as Swi3p, Rsc8p, Moira and several other uncharacterized proteins. This module, termed the SWIRM domain, is predicted to mediate specific protein-protein interactions in the assembly of chromatin-protein complexes. |
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Review
The diversity of acetylated proteins Bogdan Polevoda, Fred Sherman Genome Biology 2002, 3:reviews0006-reviews0006.6 (30 April 2002) Amino-terminal acetylation occurs on the bulk of eukaryotic acetylated proteins and on regulatory peptides, whereas lysine acetylation occurs at different positions on a variety of proteins, including histones, transcription factors, nuclear import factors, and α-tubulin. |
