ArticleThe Plant cell2002
Functional dissection of a Rice Dr1/DrAp1 transcriptional repression complex.
Article in The Plant cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- Article
- The General Transcription RepressorFrontiers in genetics · 2019Article
- The OsHAPL1-DTH8-Hd1 complex functions as the transcription regulator to repress heading date in rice.Journal of experimental botany · 2017Article
- Arabidopsis glutaredoxin S17 and its partner, the nuclear factor Y subunit C11/negative cofactor 2α, contribute to maintenance of the shoot apical meristem under long-day photoperiod.Plant physiology · 2015Article
- A negative regulator encoded by a rice WRKY gene represses both abscisic acid and gibberellins signaling in aleurone cells.Plant molecular biology · 2009Article
- Identification, characterization and interaction of HAP family genes in rice.Molecular genetics and genomics : MGG · 2008Article
- Genome-wide identification and expression analysis of the NF-Y family of transcription factors in Triticum aestivum.Plant molecular biology · 2007Article
- QTL mapping of ten agronomic traits on the soybean ( Glycine max L. Merr.) genetic map and their association with EST markers.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2004Article
- A rice WRKY gene encodes a transcriptional repressor of the gibberellin signaling pathway in aleurone cells.Plant physiology · 2004Article
- The NC2 alpha and beta subunits play different roles in vivo.Genes & development · 2002Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We characterized rice cDNA sequences for OsDr1 and OsDrAp1, which encode structural homologs of the eukaryotic general repressors Dr1 and DrAp1, respectively. OsDr1 and OsDrAp1 are nuclear proteins that interact with each other and with the TATA binding protein/DNA complex. In vitro and in vivo functional analyses showed that OsDrAp1 functions as a repressor, unlike its role in other eukaryotic systems, in which DrAp1 is a corepressor. OsDr1 and OsDrAp1 functioned together as a much stronger repressor than either one alone. Functional dissections revealed that the N-terminal histone-fold domains of OsDr1 and OsDrAp1 were necessary and sufficient for their repression and protein-protein interaction with each other. The unique glutamine- and proline-rich domain of OsDr1 had no repression activity. The basic amino acid-rich region and an arginine and glycine repeat domain of OsDrAp1 enhanced its repression activity. Thus, although OsDr1 and OsDrAp1 function as repressors, the functions of the two components are reversed compared with those of their nonplant counterparts.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.