Document Detail


A novel interaction between CCaMK and a protein containing the Scythe_N ubiquitin-like domain in Lotus japonicus.
MedLine Citation:
PMID:  21209278     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In the Rhizobium-legume symbiosis, calcium/calmodulin-dependent protein kinase (CCaMK) is a key regulator for both rhizobial infection and nodule organogenesis. Deregulation of CCaMK by either a point mutation in the autophosphorylation site or the deletion of the carboxyl-terminal regulatory domain results in spontaneous nodule formation without rhizobia. However, the underlying biochemical mechanisms are poorly understood. Here, using the kinase domain of CCaMK as a bait in yeast two-hybrid screening, we identify a novel protein, CIP73 (for CCaMK-interacting protein of approximately 73 kD), that interacts with CCaMK. CIP73 contains a Scythe_N ubiquitin-like domain and belongs to the large ubiquitin superfamily. Deletion and mutagenesis analysis demonstrate that CIP73 could only interact with CCaMK when the calmodulin-binding domain and three EF-hand motifs are removed from the kinase domain. The amino-terminal 80 amino acid residues (80-160) of CCaMK are required for interacting with CIP73 in yeast cells. On the other hand, protein pull-down assay and bimolecular fluorescence complementation assay in Nicotiana benthamiana show that the full-length CCaMK could interact with CIP73 in vitro and in planta. Importantly, CCaMK phosphorylates the amino terminus of CIP73 in a Ca2+/calmodulin-dependent manner in vitro. CIP73 transcripts are preferentially expressed in roots, and very low expression is detected in leaves, stems, and nodules. The expression in roots is significantly decreased after inoculation of Mesorhizobium loti. RNA interference knockdown of CIP73 expression by hairy root transformation in Lotus japonicus led to decreased nodule formation, suggesting that CIP73 performed an essential role in nodulation.
Authors:
Heng Kang; Hui Zhu; Xiaojie Chu; Zhenzhen Yang; Songli Yuan; Dunqiang Yu; Chao Wang; Zonglie Hong; Zhongming Zhang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-01-05
Journal Detail:
Title:  Plant physiology     Volume:  155     ISSN:  1532-2548     ISO Abbreviation:  Plant Physiol.     Publication Date:  2011 Mar 
Date Detail:
Created Date:  2011-03-02     Completed Date:  2011-05-31     Revised Date:  2013-07-03    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1312-24     Citation Subset:  IM    
Affiliation:
State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/GU980966
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
Lotus / enzymology*,  microbiology
Molecular Sequence Data
Mycorrhizae / physiology
Phenotype
Phosphorylation
Plant Proteins / chemistry*,  metabolism*
Plant Root Nodulation
Protein Binding
Protein Structure, Tertiary
Protein Transport
RNA Interference
Rhizobium / physiology
Subcellular Fractions / metabolism
Substrate Specificity
Two-Hybrid System Techniques
Chemical
Reg. No./Substance:
0/Plant Proteins; EC 2.7.11.17/Calcium-Calmodulin-Dependent Protein Kinases
Comments/Corrections

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


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