Inhibition of H3K18 deacetylation of Sirt7 by Myb-binding protein 1a (Mybbp1a)

Md Fazlul Karim, Tatsuya Yoshizawa, Yoshifumi Sato, Tomohiro Sawa, Kazuhito Tomizawa, Takaaki Akaike, Kazuya Yamagata

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)


Sirt7 localizes in the nucleus (enriched in the nucleolus) and is an NAD+-dependent deacetylase with high selectivity for the acetylated lysine 18 of histone H3 (H3K18Ac). It has been reported that Sirt7 is necessary for maintaining the fundamental properties of the cancer cell phenotype and stabilizing the tumorigenicity of human cancer via deacetylation of H3K18Ac. However, the regulators of Sirt7 deacetylase activity are unknown. Myb-binding protein 1a (Mybbp1a) is reported to interact with and regulate the function of a number of transcription factors. In the present study, we demonstrated that Mybbp1a binds to Sirt7 in vitro and in vivo. Serial deletion studies indicated that N- and C-terminal regions of Sirt7 and C-terminal region of Mybbp1a are important for the binding. Furthermore, transfection experiments showed that Mybbp1a is capable of inhibiting the deacetylation activity of H3K18Ac by Sirt7. Our findings demonstrate that Mybbp1a is a novel negative regulator of Sirt7.

Original languageEnglish
Pages (from-to)157-163
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Nov 8 2013
Externally publishedYes


  • Acetylation
  • H3K18
  • Mybbp1a
  • Sirt7
  • Sirtuin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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