Document Detail


CCA1 alternative splicing as a way of linking the circadian clock to temperature response in Arabidopsis.
MedLine Citation:
PMID:  22899064     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Most living organisms on the earth have the circadian clock to synchronize their biochemical processes and physiological activities with environmental changes to optimize their propagation and survival. CIRCADIAN CLOCK-ASSOCIATED1 (CCA1) is one of the core clock components in Arabidopsis. Notably, it is also associated with cold acclimation. However, it is largely unknown how CCA1 activity is modulated by low temperatures. We found that the CCA1 activity is self-regulated by a splice variant CCA1β and the CCA1β production is modulated by low temperatures, linking the circadian clock with cold acclimation. CCA1β competitively inhibits the activities of functional CCA1α and LATE ELONGATED HYPOCOTYL (LHY) transcription factors by forming nonfunctional CCA1α-CCA1β and LHY-CCA1β heterodimers. Consequently, CCA1β-overexpressing plants (35S:CCA1β) exhibit shortened circadian periods as observed in cca1 lhy double mutants. In addition, elongated hypocotyls and petioles and delayed flowering of CCA1α-overexpressing plants (35S:CCA1α) were rescued by coexpression of CCA1β. Interestingly, low temperatures suppress CCA1 alternative splicing and thus derepress the CCA1α activity in inducing cold tolerance. These observations indicate that a cold-responsive self-regulatory circuit of CCA1 plays a role in plant responses to low temperatures.
Authors:
Mi-Jeong Park; Pil Joon Seo; Chung-Mo Park
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-9-01
Journal Detail:
Title:  Plant signaling & behavior     Volume:  7     ISSN:  1559-2324     ISO Abbreviation:  Plant Signal Behav     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-8-17     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101291431     Medline TA:  Plant Signal Behav     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Department of Chemistry; Seoul National University; Seoul, Korea.
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