scholarly journals Proteome analysis in plant stress research: a review

2008 ◽  
Vol 43 (No. 1) ◽  
pp. 1-6 ◽  
Author(s):  
P. Vítámvás ◽  
K. Kosová ◽  
I.T. Prášil
Keyword(s):  
Plant Resistance ◽  
Posttranslational Modifications ◽  
Plant Stress ◽  
Proteome Analysis ◽  
Stress Research ◽  
Important Approach ◽  
Related Proteins ◽  
Proteomic Techniques ◽  
Identification And Quantification

Proteomic techniques that allow the identification and quantification of stress-related proteins, mapping of dynamics of their expression and posttranslational modifications represent an important approach in the research of plant stresses. In this review, we show an outline of proteomics methods and their applications in the research of plant resistance to various types of stresses.

Comparative whey proteome analysis of small-tailed Han and DairyMeade ovine milk

2021 ◽  
pp. 1-5
Author(s):  
Urhan Bai ◽  
Xiaohu Su ◽  
Zhong Zheng ◽  
Liguo Zhang ◽  
Ying Ma ◽  
...  
Keyword(s):  
Mammary Gland Development ◽  
Proteome Analysis ◽  
Dairy Sheep ◽  
Milk Traits ◽  
Beneficial Effects ◽  
Proteomic Approach ◽  
Tandem Mass Tag ◽  
Proteome Profile ◽  
Related Proteins ◽  
Gland Development

Abstract We characterized the proteome profile of mid-lactation small-tailed Han (STH) and DairyMeade (DM) ovine milk in order to explore physiological variation and differences in milk traits between the two breeds. Methodology combined a tandem mass tag (TMT) proteomic approach with LC-MS/MS technology. A total of 656 proteins were identified in STH and DM ovine milk, of which 17and 29 proteins were significantly upregulated (P < 0.05) in STH and DM, respectively. Immune-related proteins and disease-related proteins were highly expressed in STH milk, whereas S100A2 and AEBP1 were highly expressed in DM milk, which had beneficial effects on mammary gland development and milk yield. Our results provide a theoretical basis for future breeding of dairy sheep.

scholarly journals Comparative proteomic analysis of drought and high temperature response in roots of two potato cultivars

2020 ◽  
Vol 92 (2) ◽  
pp. 345-363
Author(s):  
Dominika Boguszewska-Mańkowska ◽  
Marta Gietler ◽  
Małgorzata Nykiel
Keyword(s):  
High Temperature ◽  
Stress Tolerance ◽  
High Temperatures ◽  
Protein Identification ◽  
Temperature Response ◽  
Proteome Analysis ◽  
Water Shortage ◽  
Potato Cultivars ◽  
Fine Tuning ◽  
Related Proteins

Abstract A comparative analysis of drought and high temperature responsive proteins, which means to provide insight into the molecular mechanism of potato stress tolerance. In the presented study, two potato cultivars, differing in dehydration tolerance, were compared. An analysis of their morphological, physiological and root proteome related traits proved that, although water shortage, as well as high temperatures cause the dehydration of plants, the response to those stresses at the proteome level was significantly different. LC–MS/MS protein identification showed that in roots of the sensitive cultivar, in response to drought, most changes concern increased abundance of defence- and detoxification-related proteins, while in tolerant plants, significant changes in abundance of energy and carbohydrate metabolism related proteins were observed (data are available via ProteomeXchange with identifier PXD020259). Moreover, in response to high temperatures, in the sensitive cultivar, decreased abundance of proteins involved in cell energetic metabolism was detected, while in the tolerant cultivar, the majority of proteins from this group was abundant. It can be suggested that such comparative proteome analysis indicates the fine tuning metabolism as a major factor of stress tolerance of potato plants.

A Phytotron for Plant Stress Research: How Far Can Artificial Lighting Compare to Natural Sunlight?

1996 ◽  
Vol 148 (3-4) ◽  
pp. 456-463 ◽  
Author(s):  
Stephan Thiel ◽  
Thorsten Döhring ◽  
Matthias Köfferlein ◽  
Andre Kosak ◽  
Peter Martin ◽  
...  
Keyword(s):  
Plant Stress ◽  
Natural Sunlight ◽  
Artificial Lighting ◽  
Stress Research

scholarly journals BM28, a human member of the MCM2-3-5 family, is displaced from chromatin during DNA replication.

1995 ◽  
Vol 129 (6) ◽  
pp. 1433-1445 ◽  
Author(s):  
I T Todorov ◽  
A Attaran ◽  
S E Kearsey
Keyword(s):  
Cell Cycle ◽  
Dna Replication ◽  
Posttranslational Modifications ◽  
S Phase ◽  
Present Evidence ◽  
Nuclear Binding ◽  
Eukaryotic Dna ◽  
Triton X ◽  
Related Proteins ◽  
Phase Proceeds

We have recently cloned and characterized a human member (BM28) of the MCM2-3-5 family of putative relication factors (Todorov, I.T., R. Pepperkok, R.N. Philipova, S. Kearsey, W. Ansorge, and D. Werner. 1994. J. Cell Sci. 107:253-265). While this protein is located in the nucleus throughout interphase, we report here a dramatic alteration in its nuclear binding during the cell cycle. BM28 is retained in the nucleus after Triton X-100 extraction in G1 and early S phase cells, but is progressively lost as S phase proceeds, and little BM28 is retained in detergent-extracted G2 nuclei. BM28 that is resistant to extraction in G1 nuclei is removed by DNase I digestion, suggesting that the protein is chromatin associated. In addition, we present evidence for variations in the electrophoretic mobility of BM28 that may reflect posttranslational modifications of BM28 during the cell cycle. During mitosis, BM28 is present as a fast-migrating form, but on entry into G1, the protein is converted into a slow-migrating form. With the onset of S phase, the slow-migrating form is progressively converted into the fast form. BM28 is phosphorylated at all stages of the cell cycle, but during interphase the fast form is hyperphosphorylated compared with the slow form. These apparent changes in modification may reflect or effect changes in the nuclear binding of BM28. The behavior of BM28 is not dissimilar to related proteins in Saccharomyces cerevisiae, such as Mcm2p, which are excluded from the nucleus after DNA replication. We speculate that BM28 may be involved in the control that limits eukaryotic DNA replication to one round per cell cycle.

Use of Leaf Optical Properties in Plant Stress Research

1984 ◽  
pp. 215-233 ◽  
Author(s):  
HAROLD W. GAUSMAN ◽  
JOHN J. BURKE ◽  
JERRY E. QUISENBERRY
Keyword(s):  
Optical Properties ◽  
Plant Stress ◽  
Stress Research ◽  
Leaf Optical Properties

scholarly journals Protein Prenylation in Plant Stress Responses

Molecules ◽  
2019 ◽  
Vol 24 (21) ◽  
pp. 3906 ◽  
Author(s):  
Michal Hála ◽  
Viktor Žárský
Keyword(s):  
Posttranslational Modifications ◽  
Stress Responses ◽  
Lipid Membrane ◽  
Plant Stress ◽  
Small Gtpases ◽  
Plant Responses ◽  
Protein Prenylation ◽  
Biotic Stresses ◽  
Plant Stress Responses ◽  
As Stress

Protein prenylation is one of the most important posttranslational modifications of proteins. Prenylated proteins play important roles in different developmental processes as well as stress responses in plants as the addition of hydrophobic prenyl chains (mostly farnesyl or geranyl) allow otherwise hydrophilic proteins to operate as peripheral lipid membrane proteins. This review focuses on selected aspects connecting protein prenylation with plant responses to both abiotic and biotic stresses. It summarizes how changes in protein prenylation impact plant growth, deals with several families of proteins involved in stress response and highlights prominent regulatory importance of prenylated small GTPases and chaperons. Potential possibilities of these proteins to be applicable for biotechnologies are discussed.

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