Document Detail


The light-response BTB1 and BTB2 proteins assemble nuclear ubiquitin ligases that modify phytochrome B and D signaling in Arabidopsis.
MedLine Citation:
PMID:  22732244     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Members of the Bric-a-Brac/Tramtrack/Broad Complex (BTB) family direct the selective ubiquitylation of proteins following their assembly into Cullin3-based ubiquitin ligases. Here, we describe a subfamily of nucleus-localized BTB proteins encoded by the LIGHT-RESPONSE BTB1 (LRB1) and LRB2 loci in Arabidopsis (Arabidopsis thaliana) that strongly influences photomorphogenesis. Whereas single lrb1 and lrb2 mutants are relatively normal phenotypically, double mutants are markedly hypersensitive to red light, but not to far-red or blue light, and are compromised in multiple photomorphogenic processes, including seed germination, cotyledon opening and expansion, chlorophyll accumulation, shade avoidance, and flowering time. This red light hypersensitivity can be overcome by eliminating phytochrome B (phyB) and phyD, indicating that LRB1/2 act downstream of these two photoreceptor isoforms. Levels of phyB/D proteins but not their messenger RNAs are abnormally high in light-grown lrb1 lrb2 plants, implying that their light-dependent turnover is substantially dampened. Whereas other red light-hypersensitive mutants accumulate phyA protein similar to or higher than the wild type in light, the lrb1 lrb2 mutants accumulate less, suggesting that LRB1/2 also positively regulate phyA levels in a phyB/D-dependent manner. Together, these data show that the BTB ubiquitin ligases assembled with LRB1/2 function redundantly as negative regulators of photomorphogenesis, possibly by influencing the turnover of phyB/D.
Authors:
Matthew J Christians; Derek J Gingerich; Zhihua Hua; Timothy D Lauer; Richard D Vierstra
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-06-25
Journal Detail:
Title:  Plant physiology     Volume:  160     ISSN:  1532-2548     ISO Abbreviation:  Plant Physiol.     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-09-04     Completed Date:  2013-01-10     Revised Date:  2014-06-23    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  118-34     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Apoproteins / genetics,  metabolism
Arabidopsis / genetics,  physiology,  radiation effects*
Arabidopsis Proteins / genetics,  metabolism*
Cell Nucleus / genetics,  metabolism
Color
Cotyledon / genetics,  physiology,  radiation effects
Epistasis, Genetic
Flowers / physiology
Gene Expression Regulation, Plant
Genetic Loci
Germination
Light*
Nuclear Proteins / genetics,  metabolism*
Phytochrome / genetics,  metabolism
Phytochrome B / genetics,  metabolism*
Plant Development / radiation effects
Plants, Genetically Modified / genetics,  physiology,  radiation effects
Protein Stability
Seeds / genetics,  physiology,  radiation effects
Signal Transduction*
Ubiquitin-Protein Ligases / genetics,  metabolism*
Ubiquitination
Grant Support
ID/Acronym/Agency:
GM68361/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Apoproteins; 0/Arabidopsis Proteins; 0/LRB1 protein, Arabidopsis; 0/LRB2 protein, Arabidopsis; 0/LRB3 protein, Arabidopsis; 0/Nuclear Proteins; 0/PHYB protein, Arabidopsis; 11121-56-5/Phytochrome; 136250-22-1/Phytochrome B; 158379-16-9/PHYD protein, Arabidopsis; EC 6.3.2.19/Ubiquitin-Protein Ligases
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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