STF1 is a novel TGACG-binding factor with a zinc-finger motif and a bZIP domain which heterodimerizes with GBF proteins
Cited 19 times inCited 17 times in
- STF1 is a novel TGACG-binding factor with a zinc-finger motif and a bZIP domain which heterodimerizes with GBF proteins
- Cheong, YH; Yoo, CM; Park, JM; Ryu, GR; Goekjian, VH; Nagao, RT; Key, JL; Cho, Moo Je; Hong, JC
- LEUCINE ZIPPER PROTEINS; NUCLEAR FACTOR CREB; DNA-BINDING; G-BOX; TRANSCRIPTION FACTOR; SYNTHASE PROMOTER; REGULATORY GENE; OCS-ELEMENT; PLANT GENES; COILED COIL
- Issue Date
- PLANT JOURNAL, v.15, no.2, pp.199 - 209
- Two separate nuclear binding activities (B1 and B2) in the soybean apical hypocotyl have been identified that interact with a palindromic C-box sequence (TGACGTCA) and which are developmentally regulated in an inverse manner. The bZIP factors responsible for these two binding activities, B1 and B2, were isolated from a cDNA library and designated STGA1 and STFs (STF1 and STF2), respectively. Sequence analysis shows that the STFs contain both a zinc-finger domain and a bZIP domain. The two zinc finger sequences of Cys4-Cys4 are most related to the RING zinc-finger motif carrying a Cys3-His-Cys4. In addition the bZIP domain of STFs is highly homologous to the HY5 protein of Arabidopsis. DNA binding studies revealed that STF1 binding to the TGACGT sequence requires distinct flanking sequences. Furthermore, STF1 binds to the Hex sequence as a heterodimer with G-box binding factors (GBFs), a feature not observed with STGA1. Since STF1 expression is most prevalent in apical and elongating hypocotyls, it is proposed that STF1 may be a transcription factor involved in the process of hypocotyl elongation.
- ; Go to Link
- Appears in Collections:
- BME_Journal Papers
- Files in This Item:
can give you direct access to the published full text of this article. (UNISTARs only)
Show full item record
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.