|
Philip Zegerman, Andrew J Bannister & Tony Kouzarides
Wellcome/CRC Institute and Department of Pathology, Cambridge University, Tennis Court Road, Cambridge, CB2 1QR, UK
Correspondence to: Tony Kouzarides, Wellcome/CRC Institute and Department of Pathology, Cambridge University, Tennis Court Road, Cambridge, CB2 1QR, UK
|
Acetyltransferases are essential enzymes for a wide variety of cellular processes and mutations in acetyltransferase genes have been associated with the development of certain cancers. For this reason, we conducted a computerized sequence homology search for novel acetyltransferases. Here, we show that the putative tumour suppressor protein Fus-2 has homology to the catalytic domain of acetyltransferases. We demonstrate that Fus-2 can acetylate the N-terminus of proteins using a ping-pong mechanism and that it has a specificity for substrates. Consistent with other N-acetyltransferases, Fus-2 localizes to the cytoplasm, as shown by GFP-tag experiments. Since the Fus-2 gene maps to the chromosomal region 3p21.3, which contains at least one tumour suppressor gene, the N-acetyltransferase functions of Fus-2 may be relevant to its potential role in cancer. Oncogene (2000) 19, 161 – 163.
|
