Histone cross-linking by transglutaminase

Jae Hong Kim, Kang Hoon Nam, Oh Seok Kwon, In Gyu Kim, Michael Bustin, Hyon E. Choy, Sang Chul Park

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Transglutaminases irreversibly catalyze covalent cross-linking of proteins by forming isopeptide bonds between peptide-bound glutamine and lysine residues. Among several transglutaminases, tissue-type transglutaminase (tTGase) is most ubiquitously found in every type of cells and tissues in animals, but its natural substrate has yet to be identified. In an attempt to identify the natural substrate for tTGase, we examined in vitro if core histones were subject to cross-linking by tTGase. We found core histone subunits, H2A and H2B, were specifically cross-linked by tTGase. The cross-linking was between either one or both glutamines at C-terminal end of H2A (-VTIAQ104GGVLPNTQ112SVLLPKKTESSKSK-C′ end) and the first and/or third lysine from C-terminal end of H2B (-AVESEGK116AVTKYTSSK125-C′ end). The cross-linking occurred only when these subunits were released from nucleosome but not when these were organized in nucleosome. Most interestingly, in chicken erythrocyte the cross-linked H2A-H2B was present in a significant amount. From these results, it can be proposed that tTGase-mediated cross-linking is an another form of core histone modification and it may play a role of chromatin condensation during erythrocyte differentiation.

Original languageEnglish
Pages (from-to)1453-1457
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number5
StatePublished - 4 Jul 2002


  • Core histone modification
  • Cross-linking
  • Erythrocyte
  • Transglutaminase

Cite this

Kim, J. H., Nam, K. H., Kwon, O. S., Kim, I. G., Bustin, M., Choy, H. E., & Park, S. C. (2002). Histone cross-linking by transglutaminase. Biochemical and Biophysical Research Communications, 293(5), 1453-1457. https://doi.org/10.1016/S0006-291X(02)00393-5