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Title: FUNCTIONAL ANALYSIS OF THE MDV BASIC-LEUCINE ZIPPER PRODUCT, MEQ

Author
item BRUNOVSKIS, PETER - CASE WESTERN RESERVE UNIV
item QIAN, ZHENG - CASE WESTERN RESERVE UNIV
item LI, DESHAN - CASE WESTERN RESERVE UNIV
item Lee, Lucy
item KUNG, HSING-JIEN - CASE WESTERN RESERVE UNIV

Submitted to: International Marek's Disease Symposium Abstracts and Proceedings
Publication Type: Proceedings
Publication Acceptance Date: 9/7/1996
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Through a combination of co-precipitation and gel shift analyses, we have identified both bZIP (e.g., c-Fos) and non-bZIP (e.g., p53) proteins capable of interacting with the MDV basic-leucine zipper (bZIP)-containing transcription factor, Meq. By co-immunoprecipitation analysis, we have determined that Meq-p53 interactions depend on an intact bZIP domain. Other evidence suggests that the Meq-p53 interaction domain is distinct from that of SV 40 large T antigen (e.g., p53 DNA binding domain). Further, we have investigated functional Meq interactions by transient contransfection analyses using reporter constructs containing p53- and AP- 1 (or TRE)-responsive elements linked to a minimal promoter-driven luciferase gene. These analyses have been useful in demonstrating functional interactions between Meq-Meq, Meq-p53, and Meq-Fos. In addition to transformation-associated functions, Meq may have a role in productive infections also. This is partly based on our identification of an optimal Meq binding site near the putative MDV origin of replication. Furthermore, we have characterized a genomic fusion of BamHI-H sequences to the 3'-end of Meq, specifically in the non-productive RP1 lymphoblastoid cell line. Along with recent evidence implicating Meq in transformation (1,2) the RP1-Meq results, particularly in the context of recent transactivation data, underscore Meq's potential to exhibit multiple biological functions.