Histone H2B ubiquitylation is not required for histone H3 methylation at lysine 4 in tetrahymena.
Ubiquitylation of histone H2B and/or a component of the system that ubiquitylates H2B is required for methylation of histone H3 at lysine 4 (H3K4) in yeasts and probably in humans. In this study, the single ubiquitylation site was mapped to conserved lysine 115 of the C-terminal region of histone H2B in the single-cell model organism Tetrahymena thermophila. In strains lacking H2B ubiquitylation, H3K4 methylation was not detectably affected. As in other organisms, the E2 ubiquitin-conjugating enzyme Ubc2 and the E3 ubiquitin ligase Bre1 were required for H2B ubiquitylation. However, neither enzyme was required for H3K4 methylation. These studies argue that, in T. thermophila, the histone ubiquitylation mechanism is not required for H3K4 methylation, demonstrating that different organisms can speak different languages in the "cross-talk" among post-translational modifications on different histones.
Wang
Zhe
Z
Department of Biology, University of Rochester, Rochester, New York 14627, USA.
Cui
Bowen
B
Gorovsky
Martin A
MA
D000595:Amino Acid Sequence; D000818:Animals; D016000:Cluster Analysis; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D046228:Microarray Analysis; D008969:Molecular Sequence Data; D015800:Protozoan Proteins / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D013768:Tetrahymena / Q000235:genetics / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism; D054875:Ubiquitination
D006657:Histones; D015800:Protozoan Proteins; D044767:Ubiquitin-Protein Ligases; D008239:Lysine