Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M000121200
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dc.titleA zebrafish Ftz-F1 (Fushi Tarazu Factor 1) homologue requires multiple subdomains in the D and E regions for its transcriptional activity
dc.contributor.authorLiu, D.
dc.contributor.authorChandy, M.
dc.contributor.authorLee, S.-K.
dc.contributor.authorLe Dréan, Y.
dc.contributor.authorAndo, H.
dc.contributor.authorXiong, F.
dc.contributor.authorLee, J.W.
dc.contributor.authorHew, C.L.
dc.date.accessioned2014-10-27T08:20:45Z
dc.date.available2014-10-27T08:20:45Z
dc.date.issued2000-06-02
dc.identifier.citationLiu, D., Chandy, M., Lee, S.-K., Le Dréan, Y., Ando, H., Xiong, F., Lee, J.W., Hew, C.L. (2000-06-02). A zebrafish Ftz-F1 (Fushi Tarazu Factor 1) homologue requires multiple subdomains in the D and E regions for its transcriptional activity. Journal of Biological Chemistry 275 (22) : 16758-16766. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M000121200
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/99987
dc.description.abstractA zebrafish Ftz-F1 homologue, zFF1A (zebrafish Ff1a or Nr5a2, a member of nuclear receptor superfamily) and its C-terminally truncated variant (zFF1B) were previously identified. Due to lack of the identity box (I-box) and activation function 2 (AF-2) domain, zFF1B lacks transactivation function and fails to synergize with estrogen receptor (ER) in regulating promoters. It was speculated that the I-box might be involved in the zFF1A/ER interaction. In the present study, the function of the I-box was examined. In the absence of the I-box or with an altered heptad 9, the AF-2 of zFF1A was not functional, either in the presence or absence of ER. The GST pull-down assay showed that zFF1A and its mutants exerted similar physical contacts with ER-LBD, suggesting that the 'dimerization' domain (I-box) is essential for the transcriptional activity of zFF1A. Moreover, nuclear receptor coactivator selectively activated zFF1 with the I-box but exerted no effect on zFF1B, indicating that the I-box is able to interact with the coactivators. By deletion study and analysis of the identified domains in GAL4-DNA binding domain, other regions of zFF1A critical for its AF were also delineated. Consistent with the mutation analysis, AF-2 was active only in the presence of the I-box. We also identified a novel AF domain (AF-3) located in the hinge region (amino acids 155-267), although the activity of AF-3 was inhibited by its flanking region. We suggest that the D and E regions of zFF1A possess both positive and negative transactivation functions, and interdomain 'cross-talk' may confer the full transcriptional activity of the protein.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.M000121200
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1074/jbc.M000121200
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume275
dc.description.issue22
dc.description.page16758-16766
dc.description.codenJBCHA
dc.identifier.isiut000087392200052
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