Abstract 1115 Biochemical Basis of SMYD5 in HIV Latency and Transcriptional Reactivation

SMYD5, a protein lysine methyltransferase, has been shown to regulate HIV-1 reactivation from latency. However, the biochemical mechanisms underlying this regulation remain unclear. This study aims to uncover these mechanisms by focusing on SMYD5's interactions with Transactivation Response RNA (TAR RNA) and the viral Tat protein. We hypothesize that SMYD5 influences the assembly of the transactivation complex at the HIV promoter, potentially by inducing conformational changes in TAR RNA. Gel shift assays using both full-length and truncated SMYD5 mutants revealed that SMYD5 binds weakly to TAR RNA.