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

Author
item KUNG, HSING-JIEN - UC DAVIS CANCER CENTER
item Lee, Lucy
item LIU, JUINN-LIN - CASE WESTERN RESERVE UNIV
item LIN, SU-FANG - UC DAVIS CANCER CENTER

Submitted to: International Marek's Disease Symposium Abstracts and Proceedings
Publication Type: Proceedings
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 replication functions of Marek's disease virus. It is one of the very 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 sare 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 predominantly in the nucleus, nucleolus and coiled-bodies, but occasionally 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.