The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
RAV1, a novel DNA-binding protein, binds to bipartite recognition sequence through two distinct DNA-binding domains uniquely found in higher plants
Open accessAbstract
We have cloned and characterized two novel DNA binding proteins designated RAV1 and RAV2 from Arabidopsis thaliana. RAV1 and RAV2 contain two distinct amino acid sequence domains found only in higher plant species. The N-terminal regions of RAV1 and RAV2 are homologous to the AP2 DNA-binding domain present in a family of transcription factors represented by the Arabidopsis APETALA2 and tobacco EREBP proteins, while the C-terminal region exhibits homology to the highly conserved C-terminal domain, designated B3, of VP1/ABI3 transcription factors. Binding site selection assays using a recombinant glutathione S-transferase fusion protein have revealed that RAV1 binds specifically to bipartite recognition sequences composed of two unrelated motifs, 5'-CAACA-3' and 5'-CACCTG-3', separated by various spacings in two different relative orientations. Analyses using various deletion derivatives of the RAV1 fusion protein show that the AP2 and B3-like domains of RAV1 bind autonomously to the CAACA and CACCTG motifs, respectively, and together achieve a high affinity and specificity of binding. From these results, we suggest that the AP2 and B3-like domains of RAV1 are connected by a highly flexible structure enabling the two domains to bind to the CAACA and CACCTG motifs in various spacings and orientations.
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Cited by
Sakuma, Y., Liu, Q., Dubouzet, J. G., Abe, H., Shinozaki, K., & Yamaguchi-Shinozaki, K. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.6299 · Cited by 1,993
Auxin-responsive gene expression: genes, promoters and regulatory factors
Hagen, G., & Guilfoyle, T. (2002) · Plant Molecular Biology · doi:10.1023/a:1015207114117 · Cited by 1,262
Licausi, F., Ohme‐Takagi, M., & Perata, P. (2013) · New Phytologist · doi:10.1111/nph.12291 · Cited by 1,020
Agarwal, P. K., Gupta, K., Lopato, S., & Agarwal, P. (2017) · Journal of Experimental Botany · doi:10.1093/jxb/erx118 · Cited by 283
Metadata
- Authors
- Kagaya, Y., Ohmiya, K., & Hattori, T.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 1999-01-01
- Volume
- 27
- Issue
- 2
- Pages
- 470-478
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2074106886
- Cited by
- 462
- References
- 31
- FWCI
- 11.97
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: RAV1, a novel DNA-binding protein, binds to bipartite recognition sequence through two distinct DNA-binding domains uniquely found in higher plants. https://app.cochat.ai/papers/10.1093/nar/27.2.470
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- Kagaya, Y., Ohmiya, K., & Hattori, T. (1999). RAV1, a novel DNA-binding protein, binds to bipartite recognition sequence through two distinct DNA-binding domains uniquely found in higher plants. Nucleic Acids Research. https://doi.org/10.1093/nar/27.2.470
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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