Characterization of the PR domain of RIZ1 histone methyltransferase

Céline Derunes, Klára Briknarová, Liqing Geng, Sheng Li, Chris R. Gessner, Krissi Hewitt, Shuang Ding Wu, Shi Huang, Virgil I. Woods, Kathryn R. Ely

Research output: Contribution to journalArticlepeer-review

47 Scopus citations


RIZ1 (PRDM2) and PRDI-BF1 (PRDM1) are involved in B cell differentiation and the development of B cell lymphomas. These proteins are expressed in two forms that differ by the presence or absence of a PR domain. The protein product that retains the PR domain is anti-tumorigenic while the product that lacks the PR domain is oncogenic and over-expressed in tumor cells. The conserved PR domain is homologous to the SET domain from a family of histone methyltransferases. RIZ1 is also a histone methyltransferase and methylates lysine 9 in histone H3. This activity has been mapped to the PR domain. In the present study, deuterium exchange mass spectrometry was used to define the structural boundaries of the RIZ1 PR domain and to map sites of missense mutations that occur in human cancers and reduce methyltransferase activity. Flexible segments were selectively deleted to produce protein products that crystallize for structural studies. Segments at the carboxyl terminus of the PR domain that are involved in methylation of H3 were shown to be flexible, similar to SET domains, suggesting that the PR and SET methyltransferases may belong to an emerging class of proteins that contain mobile functional regions.

Original languageEnglish
Pages (from-to)925-934
Number of pages10
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Aug 5 2005


  • Deuterium exchange
  • Histone methyltransferases
  • Mass spectrometry
  • PR domains
  • SET domains


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