GhUMC1, a blue copper-binding protein, regulates lignin synthesis and cotton immune response

2018 ◽  
Vol 504 (1) ◽  
pp. 75-81 ◽  
Author(s):  
Wan Zhu ◽  
Erlin Gao ◽  
Muhammad Shaban ◽  
Yujing Wang ◽  
Honglei Wang ◽  
...  
Keyword(s):  
Immune Response ◽  
Binding Protein ◽  
Copper Binding ◽  
Blue Copper ◽  
Lignin Synthesis ◽  
Copper Binding Protein

scholarly journals Transcription of Two Blue Copper-Binding Protein Isogenes Is Highly Correlated with Arbuscular Mycorrhizal Development in Medicago truncatula

2010 ◽  
Vol 23 (9) ◽  
pp. 1175-1183 ◽  
Author(s):  
István Parádi ◽  
Diederik van Tuinen ◽  
Dominique Morandi ◽  
Sergio Ochatt ◽  
Franck Robert ◽  
...  
Keyword(s):  
Medicago Truncatula ◽  
Time Course ◽  
Binding Protein ◽  
Quantitative Polymerase Chain Reaction ◽  
Arbuscular Mycorrhizal ◽  
Copper Binding ◽  
Wild Type ◽  
Blue Copper ◽  
Copper Binding Protein ◽  
Mycorrhizal Development

Expression profiling of two paralogous arbuscular mycorrhizal (AM)-specific blue copper-binding gene (MtBcp1a and MtBcp1b) isoforms was performed by real-time quantitative polymerase chain reaction in wild-type Medicago truncatula Jemalong 5 (J5) during the mycorrhizal development with Glomus intraradices for up to 7 weeks. Time-course analysis in J5 showed that expression of both MtBcp1 genes increased continuously and correlated strongly with the colonization intensity and arbuscule content. MtPT4, selected as a reference gene of the functional plant-fungus association, showed a weaker correlation to mycorrhizal development. In a second experiment, a range of mycorrhizal mutants of the wild-type J5 was assessed. Strictly AM-penetration-defective TRV25-C and TRV25-D (dmi3, Mtsym13), hypomycorrhizal TR25 and TR89 (dmi2, Mtsym2) mutants, and a hypermycorrhizal mutant TRV17 (sunn, Mtsym12) were compared with J5 3 and 7 weeks after inoculation. No MtBcp1 transcripts were detected in the mutants blocked at the appressoria stage. Conversely, TR25, TR89, and J5 showed a gradual increase of the expression of both MtBcp1 genes in 3- and 7-week-old plants, similar to the increase in colonization intensity and arbuscule abundance. The strong correlation between the expression level of AM-specific blue copper-binding protein-encoding genes and AM colonization may imply a basic role in symbiotic functioning for these genes, which may serve as new molecular markers of arbuscule development in M. truncatula.

scholarly journals The Prion Protein is a Combined Zinc and Copper Binding Protein:  Zn2+Alters the Distribution of Cu2+Coordination Modes

2007 ◽  
Vol 129 (50) ◽  
pp. 15440-15441 ◽  
Author(s):  
Eric D. Walter ◽  
Daniel J. Stevens ◽  
Micah P. Visconte ◽  
Glenn L. Millhauser
Keyword(s):  
Prion Protein ◽  
Binding Protein ◽  
Copper Binding ◽  
Coordination Modes ◽  
Copper Binding Protein

scholarly journals The copBL operon protects Staphylococcus aureus from copper toxicity: CopL is an extracellular membrane–associated copper-binding protein

2019 ◽  
Vol 294 (11) ◽  
pp. 4027-4044 ◽  
Author(s):  
Zuelay Rosario-Cruz ◽  
Alexander Eletsky ◽  
Nourhan S. Daigham ◽  
Hassan Al-Tameemi ◽  
G. V. T. Swapna ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Protein ◽  
Copper Toxicity ◽  
Copper Binding ◽  
Copper Binding Protein

scholarly journals Studies on the appearance of a hepatic copper-binding protein in normal and zinc-deficient rats

1976 ◽  
Vol 36 (1) ◽  
pp. 101-112 ◽  
Author(s):  
I. Bremner ◽  
N. T. Davies
Keyword(s):  
Molecular Weight ◽  
Metal Binding ◽  
Binding Protein ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Low Molecular Weight ◽  
Copper Binding ◽  
Hepatic Copper ◽  
Copper Binding Protein ◽  
Molecular Weight Form

1. A study has been made by gel-filtration techniques of the soluble copper- and zinc-binding proteins in rat liver after both intraperitoneal injection of Cu and dietary Cu supplementation.2. Liver Cu and Zn concentrations increased after injection of Cu, both metals accumulating in the cytosol, mainly in a fraction with an apparent molecular weight of (about 12 000)3. When Zn-deficient rats were injected with Cu, there was little change in liver Zn concentration and the occurrence of Cu in the low-molecular-weight form (about 12 000) was more transient. At most periods after injection, Cu accumulated mainly in a fraction with a molecular weight greater than 65 000.4. When the rats were Cu-loaded by dietary supplementation, virtually no Cu or Zn was found in the low-molecular-weight form in Zn-deficient rats, although they were found in the Zn-supplemented animals.5. The results suggest that Zn is essential for the accumulation of Cu in this form, but not for Cu to stimulate production of the metal-binding protein by a process requiring active protein synthesis.

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