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Nucleic Acids Research, Vol 27, Issue 5 1251-1262, Copyright © 1999 by Oxford University Press

ARTICLES

FBI-1, a factor that binds to the HIV-1 inducer of short transcripts (IST), is a POZ domain protein

DJ Morrison, PS Pendergrast, P Stavropoulos, SU Colmenares, R Kobayashi and N Hernandez
Undergraduate Program, Department of Pharmacology, State University of New York at Stony Brook, Stony Brook, NY 11794, USA.

The HIV-1 promoter directs the synthesis of two classes of transcripts, short, non-polyadenylated transcripts and full-length, polyadenylated transcripts. The synthesis of short transcripts is activated by a bipartite DNA element, the inducer of short transcripts or IST, located downstream of the HIV-1 transcriptional start site, while the synthesis of full-length transcripts is activated by the viral activator Tat. Tat binds to the RNA element TAR, which is encoded largely between the two IST half-elements. Upon activation by Tat, the synthesis of short RNAs is repressed. We have previously purified a factor called FBI-1 (for factor that binds to IST) whose binding to wild-type and mutated ISTs correlated well with the abilities of these ISTs to direct the synthesis of short transcripts. Here, we report the cloning of cDNAs encoding FBI-1. FBI-1 contains a POZ domain at its N-terminus and four Kruppel-type zinc fingers at its C-terminus. The C-terminus is sufficient for specific binding, and FBI-1 can form homomers through its POZ domain and, in vivo, through its zinc finger domain as well. In addition, FBI-1 associates with Tat, suggesting that repression of the short transcripts by Tat may be mediated through interactions between the two factors.
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