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J Biol Chem, Vol. 273, Issue 36, 23335-23343, September 4, 1998
Department of Molecular Biology, Göteborg University,
Medicinaregatan 9C, Box 462, S-405 30 Göteborg, Sweden
Forkhead-related activator 2 (FREAC-2) is a human
transcription factor expressed in lung and placenta that binds to
cis-elements in several lung-specific genes. We have
identified the parts of FREAC-2 responsible for
trans-activation and found two functionally redundant
activation domains on the C-terminal side of the DNA binding forkhead
domain. Activation domain 1 consists of the most C-terminal 23 amino
acids of FREAC-2 and contains a sequence motif conserved in an
activation domain of another forkhead protein, FREAC-1. Activation
domain 2 is built up by three synergistic subdomains in the central
part of the FREAC-2 protein. FREAC-2 was shown to interact in
vitro with TBP and TFIIB. The target site for FREAC-2 on TBP was
localized to the N-terminal repeat in the core domain of TBP. TFIIB
binds FREAC-2 close to the cleft between its two globular domains. The
part of FREAC-2 that binds TBP was mapped to 21 amino acids in the
C-terminal end of the forkhead domain. This sequence is well conserved
among forkhead proteins, raising the possibility that interaction with
TBP may be a general characteristic of this family of transcription
factors. Overexpression of TFIIB potentiates activation by FREAC-2 in a manner dependent on the FREAC-2 activation domains. Nuclear
localization of FREAC-2 was found to depend on sequences from both ends
of the forkhead domain.
The Human Forkhead Protein FREAC-2 Contains Two Functionally
Redundant Activation Domains and Interacts with TBP and TFIIB
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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