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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao The Plant Journalarrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
The Plant Journal
Article . 2012 . Peer-reviewed
License: Wiley Online Library User Agreement
Data sources: Crossref
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The RS domain of Arabidopsis splicing factor RRC1 is required for phytochrome B signal transduction

Authors: Hiromasa, Shikata; Mami, Shibata; Tomokazu, Ushijima; Moeko, Nakashima; Sam-Geun, Kong; Ken, Matsuoka; Chentao, Lin; +1 Authors

The RS domain of Arabidopsis splicing factor RRC1 is required for phytochrome B signal transduction

Abstract

Summary Plants monitor the light environment through informational photoreceptors that include phytochromes. In seedling de‐etiolation, phytochrome B (phyB), which is the most important member of the phytochrome family, interacts with transcription factors to regulate gene expression and transduce light signals. In this study, we identified rrc1 ( reduced red‐light responses in cry1cry2 background 1 ), an Arabidopsis mutant that is impaired in phyB‐mediated light responses. A genetic analysis demonstrated that RRC1 affected light signaling in a phyB‐dependent manner. RRC1 encodes an ortholog of the human potential splicing factor SR140. The RRC1 polypeptide contains a C‐terminal arginine/serine‐rich (RS) domain that is important for the regulation of alternative splicing. Although the complete loss of RRC1 caused pleiotropic developmental abnormalities, the deletion of the RS domain specifically reduced phyB signaling and caused aberrant alternative splicing of several SR protein genes. Moreover, semi‐quantitative RT‐PCR analysis revealed that the alternative splicing patterns of some of the SR protein genes were altered in a red‐light‐dependent manner, and that these responses were reduced in both phyB and rrc1 mutants. These findings suggest that the regulation of alternative splicing by the RS domain of RRC1 plays an important role in phyB signal transduction.

Related Organizations
Keywords

Cell Nucleus, Light, Arabidopsis Proteins, Active Transport, Cell Nucleus, Arabidopsis, Color, Genetic Pleiotropy, Genes, Plant, Plants, Genetically Modified, Protein Structure, Tertiary, Alternative Splicing, Transformation, Genetic, Gene Expression Regulation, Plant, Phytochrome B, RNA, Messenger, Cloning, Molecular, Plasmids, Sequence Deletion, Signal Transduction

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Powered by OpenAIRE graph
citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
56
Top 10%
Top 10%
Top 10%