The most studied members of HAT of type B are HAT1 and HAT4 [32, 33].
Tafrov, "Human histone acetyltransferase 1 (Hat1) acetylates lysine 5 of histone H2A in vivo," Molecular and Cellular Biochemistry, vol.
H4 replication- dependent diacetylation and Hat1
promote S-phase chromatin assembly in vivo.
The expression levels of HAT1 and p300, histone acetyltransferases, in nucleus were constant regardless of the presence of scopoletin.
Furthermore, it was observed in our study that the expression of HAT1, a histone acetyltransferase, is not changed by scopoletin but the expression of histone deacetyltransferases such as HDAC1, SIRT1 and SIRT6 are increased in human lung fibroblasts.
Such protein acyltransferase function was also ascribed to HATs such as HAT1
, CBP, and p300 which were also found to accommodate higher acyl group donors such as propionyl CoA and butyryl CoA .
The cytoplasmic type B HATs are responsible for deposition-related acetylation of free histone substrates only a few B-HATs have been characterized, including HAT1
, HAT2 , Rtt109 , HatB3.1 , and HAT4 .
The array analysis implicated a number of novel genes for response to [O.sub.3] in [Il10.sup.+/+] and [Il10.sup.-/-] mice, including Il33 and Hat1
. IL-33 is a member of the IL-1 superfamily and is expressed on epithelial cells.