Alternatively, SseF-TIP60 interaction may alter the acetylation activity of TIP60, thus affecting TIP60 related functions. Supporting this hypothesis, our preliminary in vitro acetylation assays suggest that SseF increased the histone acetylation activity of TIP60, especially for histone H2. Histone is the only known substrate for Tip60. Total histone acetylation

was not increased in infected cells (data not shown). This is consistent with the low amount of SseF translocated. It is possible that local SseF concentration may be higher in infected cells. Although TIP60 is not known to be learn more directly involved in vesicle trafficking, it is possible that TIP60 affected histone acetylation leading to altered expression of trafficking-related proteins. Interestingly, our preliminary data showed that knock down of TIP60 reduced continuous Sif formation, a phenotype Temsirolimus mouse similar to that of the sseF null mutant (Additional file 1: Fig. S1). Future experiments are required to determine whether the increase in histone acetylation leads to increases in TIP60-mediated downstream functions. This may ultimately

help us to understand how SseF interact with TIP60 to promote Salmonella replication inside the host cells. Conclusions We found that TIP60, an acetyltransferase, interacts with Salmonella SseF. We further showed that the TIP60 acetylation activity was increased in the presence of SseF, and TIP60 was upregulated upon Salmonella infection. More importantly, TIP60 is required selleck kinase inhibitor for efficient intracellular Thiamet G Salmonella replication in macrophages. Our study demonstrated that Salmonella may use SseF to exploit the host TIP60 acetyltransferase activity to promote efficient Salmonella replication inside host cells. Acknowledgements Research was supported by NSFC grant 30628001 to D. Z., and

by “”863″” grant 2006AA02A253 to D.Q. Electronic supplementary material Additional file 1: TIP60 is required for continuous Salmonella -induced filament formation. HeLa cells were transfected with a plasmid expressing TIP60 siRNA or a control vector expressing the scrambled siRNA. Transfected cells were infected with wild-type Salmonella. Infected cells were stained for TIP60 (red) or LAMP2 (green). Arrows indicates Sifs, and arrowheads indicate the “”pseudo-Sifs”". (TIFF 575 KB) References 1. Utley RT, Cote J: The MYST family of histone acetyltransferases. Curr Top Microbiol Immunol 2003, 274:203–236.PubMed 2. Ikura T, Ogryzko VV, Grigoriev M, Groisman R, Wang J, Horikoshi M, Scully R, Qin J, Nakatani Y: Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 2000,102(4):463–473.PubMedCrossRef 3. Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G: Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. Virology 1996,216(2):357–366.PubMedCrossRef 4.