TY - JOUR
T1 - Paramecium bursaria chlorella virus 1 encodes a polyamine acetyltransferase
AU - Charlop-Powers, Zachary
AU - Jakoncic, Jean
AU - Gurnon, James R.
AU - Van Etten, James L.
AU - Zhou, Ming Ming
PY - 2012/3/16
Y1 - 2012/3/16
N2 - Paramecium bursaria chlorella virus 1 (PBCV-1), a large DNA virus that infects green algae, encodes a histone H3 lysine 27-specific methyltransferase that functions in global transcriptional silencing of the host. PBCV-1 has another gene a654l that encodes a protein with sequence similarity to the GCN5 family histone acetyltransferases. In this study, we report a 1.5 Å crystal structure of PBCV-1 A654L in a complex with coenzyme A. The structure reveals a unique feature of A654L that precludes its acetylation of histone peptide substrates. We demonstrate that A654L, hence named viral polyamine acetyltransferase (vPAT), acetylates polyamines such as putrescine, spermidine, cadaverine, and homospermidine present in both PBCV-1 and its host through a reaction dependent upon a conserved glutamate 27. Our study suggests that as the first virally encoded polyamine acetyltransferase, vPAT plays a possible key role in the regulation of polyamine catabolism in the host during viral replication.
AB - Paramecium bursaria chlorella virus 1 (PBCV-1), a large DNA virus that infects green algae, encodes a histone H3 lysine 27-specific methyltransferase that functions in global transcriptional silencing of the host. PBCV-1 has another gene a654l that encodes a protein with sequence similarity to the GCN5 family histone acetyltransferases. In this study, we report a 1.5 Å crystal structure of PBCV-1 A654L in a complex with coenzyme A. The structure reveals a unique feature of A654L that precludes its acetylation of histone peptide substrates. We demonstrate that A654L, hence named viral polyamine acetyltransferase (vPAT), acetylates polyamines such as putrescine, spermidine, cadaverine, and homospermidine present in both PBCV-1 and its host through a reaction dependent upon a conserved glutamate 27. Our study suggests that as the first virally encoded polyamine acetyltransferase, vPAT plays a possible key role in the regulation of polyamine catabolism in the host during viral replication.
UR - http://www.scopus.com/inward/record.url?scp=84858596006&partnerID=8YFLogxK
U2 - 10.1074/jbc.C111.337816
DO - 10.1074/jbc.C111.337816
M3 - Article
C2 - 22277659
AN - SCOPUS:84858596006
SN - 0021-9258
VL - 287
SP - 9547
EP - 9551
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 12
ER -