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Title: A COMPARATIVE STUDY OF BZIP PROTEINS IN ONCOGENIC HERPESVIRUSES: MEQ AND K-BZIP

Author
item KUNG, H - UC DAVIS CANCER CENTER
item ROBINSON, D - UC DAVIS CANCER CENTER
item KAMIL, J - CASE WESTERN RES UNIV
item LIU, L - USDA ADOL EAST LANSING MI
item LI, D.-S - USDA ADOL EAST LANSING MI
item Lee, Lucy
item LIN, S - USDA ADOL EAST LANSING MI

Submitted to: World Poultry Congress Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: 8/20/2000
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Meq is a bZIP (basic leucine zipper) transcriptional factor implicated in the transformation and replications functions of Marek's disease virus. It is one of the few genes expressed consistently in latent and tumor cells. Our previous work has defined the DNA recognition sequences (MERE I and II) and the transactivation/repression domain of Meq. Meq binding sites are found not only in its own promoter, but also near the replication origin. The zip domain of Meq allows it to dimerize with a variety of ZIP proteins including Jun, Fos, ATF2 and CREB, such that it has the ability to modulate the functions of other cellular factors and to diversify the DNA binding capacity. Meq is found to be located predominatly in the nucleus, nucleolus and coiled bodied, but occasional in the nuclear periphery in a cell cycle and phosphorylation dependent manner. We recently reported that this phosphorylation is carried out by CDK2 at Serine 42 of Meq, a residue located in the middle of the two basic regions of Meq (Liu et al., J Virol 1999). This phosphorylation significantly diminishes the DNA binding capacity of Meq, which may account for its lack of retention in the nucleus. Like other herpesvirus gene products, Meq may function both in the nucleus as well as in the cytoplasm, to effect the transformation and anti apoptosis effects.