Abstract:
:A yeast two-hybrid screen has identified HBP1 as a transcription factor capable of interacting with the pocket protein family. We show that HBP1 can interact with one of these, RB, both in vitro and in mammalian cells. Two distinct RB binding sites are present within HBP1--a high affinity binding site, mediated by an LXCXE motif and a separate low affinity binding site present within an activation domain. GAL4-fusion experiments indicate that HBP1 contains a masked activation domain. Deletion of two independent N- and C-terminal inhibitor domains unmasks an activation domain which is 100-fold more active than the full length protein. The released activation capacity is repressed by RB, p130 and p107. In addition, E1A can repress the activity of HBP1 via conserved region 1 sequences in a manner independent of the CBP co-activator. We show by stable expression in NIH3T3 cells that HBP1 has the capacity to induce morphological transformation of cells in culture.
journal_name
Oncogenejournal_title
Oncogeneauthors
Lavender P,Vandel L,Bannister AJ,Kouzarides Tdoi
10.1038/sj.onc.1201243subject
Has Abstractpub_date
1997-06-05 00:00:00pages
2721-8issue
22eissn
0950-9232issn
1476-5594journal_volume
14pub_type
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