Root plasma membrane H+-ATPase is involved in low pH-inhibited nitrogen accumulation in tea plants (Camellia sinensis L.)

2018 ◽  
Vol 86 (3) ◽  
pp. 423-432 ◽  
Author(s):  
Xianchen Zhang ◽  
Linmu Chen ◽  
Honghong Wu ◽  
Linlin Liu ◽  
Xiaochun Wan
Keyword(s):  
Plasma Membrane ◽  
Camellia Sinensis ◽  
Low Ph ◽  
Nitrogen Accumulation ◽  
Tea Plants ◽  
Root Plasma Membrane

scholarly journals Biochemical characterization of specific Alanine Decarboxylase (AlaDC) and its ancestral enzyme Serine Decarboxylase (SDC) in tea plants (Camellia sinensis)

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Peixian Bai ◽  
Liyuan Wang ◽  
Kang Wei ◽  
Li Ruan ◽  
Liyun Wu ◽  
...  
Keyword(s):  
Gene Duplication ◽  
Camellia Sinensis ◽  
Biochemical Characterization ◽  
Specific Activity ◽  
Protein Sequences ◽  
Biochemical Properties ◽  
High Similarity ◽  
New Gene ◽  
Tea Plants

Abstract Background Alanine decarboxylase (AlaDC), specifically present in tea plants, is crucial for theanine biosynthesis. Serine decarboxylase (SDC), found in many plants, is a protein most closely related to AlaDC. To investigate whether the new gene AlaDC originate from gene SDC and to determine the biochemical properties of the two proteins from Camellia sinensis, the sequences of CsAlaDC and CsSDC were analyzed and the two proteins were over-expressed, purified, and characterized. Results The results showed that exon-intron structures of AlaDC and SDC were quite similar and the protein sequences, encoded by the two genes, shared a high similarity of 85.1%, revealing that new gene AlaDC originated from SDC by gene duplication. CsAlaDC and CsSDC catalyzed the decarboxylation of alanine and serine, respectively. CsAlaDC and CsSDC exhibited the optimal activities at 45 °C (pH 8.0) and 40 °C (pH 7.0), respectively. CsAlaDC was stable under 30 °C (pH 7.0) and CsSDC was stable under 40 °C (pH 6.0–8.0). The activities of the two enzymes were greatly enhanced by the presence of pyridoxal-5′-phosphate. The specific activity of CsSDC (30,488 IU/mg) was 8.8-fold higher than that of CsAlaDC (3467 IU/mg). Conclusions Comparing to CsAlaDC, its ancestral enzyme CsSDC exhibited a higher specific activity and a better thermal and pH stability, indicating that CsSDC acquired the optimized function after a longer evolutionary period. The biochemical properties of CsAlaDC might offer reference for theanine industrial production.

Electrostatic analysis of effects of ions on the inhibition of corn root plasma membrane Mg2+-ATPase by the bivalent orthovanadate

1989 ◽  
Vol 979 (1) ◽  
pp. 46-52 ◽  
Author(s):  
Rémy Gibrat ◽  
Jean-Pierre Grouzis ◽  
Jacqueline Rigaud ◽  
Nathalie Galtier ◽  
Claude Grignon
Keyword(s):  
Plasma Membrane ◽  
Corn Root ◽  
Root Plasma Membrane

A mass spectrometric approach to identify arbuscular mycorrhiza-related proteins in root plasma membrane fractions

PROTEOMICS ◽  
2006 ◽  
Vol 6 (S1) ◽  
pp. S145-S155 ◽  
Author(s):  
Benoît Valot ◽  
Luc Negroni ◽  
Michel Zivy ◽  
Silvio Gianinazzi ◽  
Eliane Dumas-Gaudot
Keyword(s):  
Plasma Membrane ◽  
Arbuscular Mycorrhiza ◽  
Mass Spectrometric ◽  
Mass Spectrometric Approach ◽  
Related Proteins ◽  
Root Plasma Membrane

scholarly journals The Protective Effect of Exogenous Putrescine in the Response of Tea Plants (Camellia sinensis) to Salt Stress

HortScience ◽  
2018 ◽  
Vol 53 (11) ◽  
pp. 1640-1646 ◽  
Author(s):  
Fei Xiong ◽  
Jieren Liao ◽  
Yuanchun Ma ◽  
Yuhua Wang ◽  
Wanping Fang ◽  
...  
Keyword(s):  
Salt Stress ◽  
Camellia Sinensis ◽  
Effective Means ◽  
Plant Performance ◽  
Photosynthetic Parameters ◽  
Activity Levels ◽  
Salinity Treatment ◽  
Ros Scavenging ◽  
Stress Levels ◽  
Tea Plants

Camellia sinensis cultivars were treated with 5 mm putrescine (Put) under a range of sodium chloride (NaCl) concentrations. Plant performance, as indicated by various indicators associated with plant growing condition such as photosynthetic parameters and polyamine (PA) contents, especially the content of Put, was improved by the treatment. The extent of both Na+ accumulation and K+ loss increased. The activity levels of the antioxidant enzymes related to salt stress, such as superoxide dismutase (SOD), peroxidase (POD), and catalase, were significantly altered with different salt stress levels and showed a decrease in the general trend. Besides, tea polyphenols, the tea quality indicator, increased during the salinity treatment but decreased when we applied Put. These findings suggest that treatment with Put might constitute an effective means for alleviating salinity stress–induced injury through its positive effect on photosynthetic efficiency and for controlling reactive oxygen species (ROS) scavenging ability under appropriate salt stress levels.

scholarly journals Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)

1989 ◽  
Vol 261 (1) ◽  
pp. 289-291 ◽  
Author(s):  
P A Deddish ◽  
R A Skidgel ◽  
E G Erdös
Keyword(s):  
Plasma Membrane ◽  
Low Ph ◽  
Co2 Activation ◽  
Inhibitor Binding ◽  
Carboxypeptidase B ◽  
Acid Ph ◽  
Carboxypeptidase H ◽  
Membrane Bound ◽  
Carboxypeptidase N ◽  
Carboxypeptidase M

Carboxypeptidases H and M differ in their distribution and other properties, but both are activated by Co2+ and inhibited by guanidinoethylmercaptosuccinic acid. The higher degree of activation or inhibition of carboxypeptidase H by these agents at acid pH has been employed to identify this enzyme in tissues. We found that the activation or inhibition of both purified and plasma-membrane-bound human carboxy-peptidase M depends on the pH of the medium. CoCl2 activated over 6-fold at pH 5.5, but less than 2-fold at pH 7.5. Guanidinoethylmercaptosuccinic acid inhibited the membrane-bound carboxypeptidase M more effectively than the purified enzyme, and the IC50 was about 25-30 times lower at pH 5.5. As purified human plasma carboxypeptidase N and pancreatic carboxypeptidase B were also activated more at pH 5.5, we conclude that the increased activation by CoCl2 is due to the enhanced dissociation of Zn2+ below the pKa of the ligands that co-ordinate the cofactor in the protein. Thus increased activation or inhibition at acid pH would not differentiate basic carboxypeptidases.

scholarly journals Molecular Identification and Characterization of Hydroxycinnamoyl Transferase in Tea Plants (Camellia sinensis L.)

2018 ◽  
Vol 19 (12) ◽  
pp. 3938 ◽  
Author(s):  
Chi-Hui Sun ◽  
Chin-Ying Yang ◽  
Jason Tzen
Keyword(s):  
Abiotic Stress ◽  
Amino Acid ◽  
Camellia Sinensis ◽  
Polymerase Chain Reaction Analysis ◽  
Coffea Canephora ◽  
Tea Plant ◽  
Amino Acid Sequences ◽  
Hibiscus Cannabinus ◽  
Expression Level ◽  
Tea Plants

Tea (Camellia sinensis L.) contains abundant secondary metabolites, which are regulated by numerous enzymes. Hydroxycinnamoyl transferase (HCT) is involved in the biosynthesis pathways of polyphenols and flavonoids, and it can catalyze the transfer of hydroxyconnamoyl coenzyme A to substrates such as quinate, flavanol glycoside, or anthocyanins, thus resulting in the production of chlorogenic acid or acylated flavonol glycoside. In this study, the CsHCT gene was cloned from the Chin-Shin Oolong tea plant, and its protein functions and characteristics were analyzed. The full-length cDNA of CsHCT contains 1311 base pairs and encodes 436 amino acid sequences. Amino acid sequence was highly conserved with other HCTs from Arabidopsis thaliana, Populus trichocarpa, Hibiscus cannabinus, and Coffea canephora. Quantitative real-time polymerase chain reaction analysis showed that CsHCT is highly expressed in the stem tissues of both tea plants and seedlings. The CsHCT expression level was relatively high at high altitudes. The abiotic stress experiment suggested that low temperature, drought, and high salinity induced CsHCT transcription. Furthermore, the results of hormone treatments indicated that abscisic acid (ABA) induced a considerable increase in the CsHCT expression level. This may be attributed to CsHCT involvement in abiotic stress and ABA signaling pathways.

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