High impact information on MYST2

• When Hbo1 expression was inhibited in human cells, Mcm2-7 failed to associate with chromatin even though ORC and Cdc6 loading was normal [1].
• Here, we show that Hbo1, a member of the MYST histone acetyltransferase family, is a previously unrecognized positive regulatory factor for pre-RC assembly [1].
• This suppressor mutation was located in the HBO1 zinc finger [2].
• Transient transfection experiments revealed that HBO1 specifically repressed AR-mediated transcription in both CV-1 and PC-3 cells [3].
• HBO1 belongs to the MYST family, which is characterized by a highly conserved C2HC zinc finger and a putative histone acetyltransferase domain [3].

Biological context of MYST2

• Disruption of ORC2, MCM5, and HBO1 expression by small interfering RNA reduced LANA-dependent DNA replication of TR-containing plasmids [4].

Anatomical context of MYST2

• Immunofluorescence experiments showed that HBO1 is a nuclear protein, and Northern blot analysis revealed that it is ubiquitously expressed, with the highest levels present in human testis [3].
• CDK11(p58) and HBO1 colocalize in the cell nucleus [5].

Associations of MYST2 with chemical compounds

• HBO1 was found also to interact through its NTD with SRC-1a in the absence of steroid receptor [6].
• Importantly, real-time RT-PCR analysis also revealed that HBO1 enhanced SRC-1 coactivation of PR-dependent transcription of human endogenous genes such as alpha-6 integrin and 11beta-hydroxydehydrogenase 2 but not that of amphiregulin [6].
• Mutational analysis showed that the N-terminal serine-rich region of HBO1 but not the acetyltransferase function was required for inhibition [7].
• Using this method, the characterization, separation, and quantitative detection of a mixture of six naturally occurring 1,4-benzoxazin-3(4H)-one derivatives, including the hydroxamic acids (DIMBOA, DIBOA), lactams (HBOA, and HMBOA), benzoxazilinones (BOA, MBOA), and two synthetic methoxylated variations of DIBOA and HBOA, was achieved [8].

Other interactions of MYST2

• A ligand-enhanced interaction between AR and HBO1 was further confirmed in vivo and in vitro [3].
• The HBO1 N-terminal region (aa 1-340) associates additionally with PR ligand-binding domain (LBD) [6].

References