Open AccessFunctional analysis of the activation domain of RF2a, a rice transcription factor
Author(s) -
Isabel Ordiz M.,
Yang Jaemo,
Brad Barbazuk W.,
Beachy Roger N.
Publication year - 2010
Publication title -
plant biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.525
H-Index - 115
eISSN - 1467-7652
pISSN - 1467-7644
DOI - 10.1111/j.1467-7652.2010.00520.x
Subject(s) - biology , transcription factor , reporter gene , gene , transcription (linguistics) , zinc finger , amino acid , activator (genetics) , promoter , b3 domain , effector , arabidopsis , microbiology and biotechnology , gene expression , dna binding protein , genetics , mutant , linguistics , philosophy
Summary Rice transcription factor RF2a binds to the BoxII cis element of the promoter of rice tungro bacilliform virus and activates promoter expression. The acidic acid‐rich domain of RF2a is a transcription activator and has been partially characterized (Dai et al. , 2003). The RF2a acidic domain (A; amino acids 49–116) was fused with the synthetic zinc finger ZF‐TF 2C7 and was co‐introduced with a reporter gene into transgenic Arabidopsis plants. Expression of the reporter gene was increased up to seven times by the effector. In transient assays in tobacco BY‐2 protoplasts, we identified a subdomain comprising amino acids 56–84 (A5) that was equally as effective as an activator as the entire acidic domain. A chemically inducible system was used to show determined that A and A5 domains are equally as effective in transcription activation as the well‐characterized VP16 activation domain. Bioinformatics analyses revealed that the A5 domain is present only in b‐ZIP transcription factors. In dicots, the A domain contains an insertion of four amino acids that is not present in monocot proteins. The A5 domain, and similar domains in other b‐ZIP transcription factors, is predicted to form an anti‐parallel beta sheet structure.