Acetylation Site of Delta Antigen

We have demonstrated that HDAg was acetylated in vivo and in vitro (Mu et al. 2004). Notably, S-HDAg acetylated in vitro by p300 was used for MASS analysis, which identified K72 as the acetylation site. Nevertheless, we cannot rule out the possibility that, in addition to K72, S-HDAg might also contain other sites that could be acetylated by p300 or other acetyltransferases. This phenomenon occurs on some cellular proteins such as p53 (Brooks and Gu 2003) and YY1 (Yao et al. 2001), or viral proteins such as HIV-1 Tat (Kiernan et al. 1999). These proteins were found to possess multiple acetylation sites and were acetylated by several HATs. Furthermore, the common acetylation motif of nuclear receptors, KXKK (Fu et al. 2004), is also present within amino acids 36-43 of HDAg. Thus, further study is required to verify the candidate K72 and other possible unidentified acetylation sites.

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