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Title: MtMOT1.2 is responsible for molybdate supply to Medicago truncatula nodules: MtMOT1.2 delivers Mo to nodules
NSF-PAR ID:
10065413
Author(s) / Creator(s):
 ;  ;  ;  ;  ;  ;  
Publisher / Repository:
Wiley-Blackwell
Date Published:
Journal Name:
Plant, Cell & Environment
Volume:
42
Issue:
1
ISSN:
0140-7791
Page Range / eLocation ID:
p. 310-320
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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  1. Summary

    Cu+‐chaperones are a diverse group of proteins that allocate Cu+ions to specific copper proteins, creating different copper pools targeted to specific physiological processes.

    Symbiotic nitrogen fixation carried out in legume root nodules indirectly requires relatively large amounts of copper, for example for energy delivery via respiration, for which targeted copper deliver systems would be required.

    MtNCC1 is a nodule‐specific Cu+‐chaperone encoded in theMedicago truncatulagenome, with a N‐terminus Atx1‐like domain that can bind Cu+with picomolar affinities. MtNCC1 is able to interact with nodule‐specific Cu+‐importer MtCOPT1.MtNCC1is expressed primarily from the late infection zone to the early fixation zone and is located in the cytosol, associated with plasma and symbiosome membranes, and within nuclei. Consistent with its key role in nitrogen fixation,ncc1mutants have a severe reduction in nitrogenase activity and a 50% reduction in copper‐dependent cytochromecoxidase activity.

    A subset of the copper proteome is also affected in thencc1mutant nodules. Many of these proteins can be pulled down when using a Cu+‐loaded N‐terminal MtNCC1 moiety as a bait, indicating a role in nodule copper homeostasis and in copper‐dependent physiological processes. Overall, these data suggest a pleiotropic role of MtNCC1 in copper delivery for symbiotic nitrogen fixation.

     
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  2. null (Ed.)