Programmed cell death during flower senescence: isolation and characterization of cysteine proteinases from Sandersonia aurantiaca

2002 ◽  
Vol 29 (9) ◽  
pp. 1055 ◽  
Author(s):  
Jocelyn R. Eason ◽  
Dacey J. Ryan ◽  
Tatyana T. Pinkney ◽  
Erin M. O'Donoghue
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Soluble Protein ◽  
Cysteine Proteinase ◽  
Flower Senescence ◽  
Cysteine Proteinases ◽  
Cysteine Protease Inhibitors ◽  
Homologous Proteins ◽  
Isolation And Characterization ◽  
C Terminus

Cysteine protease inhibitors delayed the senescence of Sandersonia aurantiaca Hook. flowers. Tepal fading and wilting occurred later in the 2,2� -dipyridyl-treated flowers, and these flowers had a greater soluble protein content and less active endoproteases compared with control flowers that were held in water. Biochemical analysis revealed the presence of several protease-active bands in the soluble protein fraction of Sandersonia tepals. Activity of the polypeptides increased as flower senescence progressed. Western analysis with an antibody raised against the castor bean cysteine proteinase identified homologous proteins in Sandersonia flowers (ca 46, 41 and 31�kDa). Three cDNAs encoding cysteine proteinases were isolated from Sandersonia tepals (PRT5, PRT15 and PRT22). Expression of all three increased in tepals as senescence progressed. mRNAs for PRT5 were detected only in senescing flower tissue, whereas PRT15 and PRT22 were expressed in leaf, stem and root tissue. PRT5 has significant homology to C-terminus KDEL proteins, which have a role in the degradation of plant cell contents during programmed cell death. PRT15 is most similar to cysteine proteinases with a long C-terminal extension, whereas PRT22 is homologous to stress-induced cysteine proteinases.

scholarly journals Bax Inhibitor 1 (BI-1) as a conservative regulator of Programmed Cell Death

2019 ◽  
Vol 73 ◽  
pp. 681-702
Author(s):  
Mirosław Godlewski ◽  
Agnieszka Kobylińska
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Actin Polymerization ◽  
Functional Condition ◽  
Sphingolipid Metabolism ◽  
Antiapoptotic Proteins ◽  
Crop Tolerance ◽  
Cellular Processes ◽  
C Terminus ◽  
Suicidal Death

Programmed cell death (PCD) is a physiological process in which infected or unnecessary cells due to their suicidal death capability can be selectively eliminated. Pro- and antiapoptotic proteins play an important role in the induction or inhibition of this process. Presented article shows property of Bax-1 (BI-1) inhibitor which is one of the conservative protein associated with the endoplasmic reticulum (ER) as well as its cytoprotective role in the regulation of cellular processes. It was shown that: 1) BI-1 is a small protein consisting of 237 amino acids (human protein - 36 kDa) and has 6 (in animals) and 7 (in plants) α-helical transmembrane domains, 2) BI-1 is expressed in all organisms and in most tissues, moreover its level depends on the functional condition of cells and it is involved in the development or reaction to biotic and abiotic stresses, 3) BI-1 forms a pH-dependent Ca2+ channel enabling release of these ions from the ER, 4) cytoprotective effects of BI-1 requires a whole, unchanged C-terminus, 5) BI-1 can interact directly with numerous other proteins, BI-1 protein affects numerous cellular processes, including: counteracting ER stress, oxidative stress, loss of cellular Ca2+ homeostasis as well as this protein influences on sphingolipid metabolism, autophagy, actin polymerization, lysosomal activity and cell proliferation. Studies of BI-1 functions will allow understanding the mechanisms of anticancer therapy or increases the knowledge of crop tolerance to environmental stresses.

scholarly journals Changes in Proteolytic Activity and Cysteine Proteinase Gene Expression during the Senescence of etr1-1 Transgenic Petunias

HortScience ◽  
2005 ◽  
Vol 40 (4) ◽  
pp. 1105B-1105
Author(s):  
Michelle Jones ◽  
Gunching Chaffin ◽  
David Clark
Keyword(s):  
Proteolytic Activity ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Transcript Abundance ◽  
Flower Senescence ◽  
Cysteine Proteinases ◽  
University Of Florida ◽  
Nitrogen Levels ◽  
Protein Levels ◽  
The University

Corolla senescence in petunias was accompanied by a decrease in total proteins and a corresponding increase in proteolytic activity. Transgenic petunias that contain the mutated ethylene receptor (35S:etr1-1) have reduced sensitivity to ethylene and delayed flower senescence. Declines in total protein levels and increases in proteolytic activity were also delayed in etr1-1 flowers and corresponded with corolla wilting. Experiments using class-specific proteinase inhibitors indicated that proteolytic activity in petunia corollas was largely due to cysteine proteinases. Total nitrogen levels within the corollas of both wild type and etr1-1 flowers also decreased during senescence. Nine cDNAs encoding putative cysteine proteinases (CPs) were identified from a petunia EST database developed at the University of Florida. Six of these cysteine proteinases showed increased transcript abundance during corolla senescence (senescence-associated CPs) while three decreased in abundance. Of the six senescence-associated cysteine proteinases, only five showed delayed up regulation in etr1-1 flowers that corresponded with corolla wilting. The role of ethylene in the regulation of protein degradation during flower senescence will be discussed.

PLANT PROGRAMMED CELL DEATH, ETHYLENE AND FLOWER SENESCENCE

2005 ◽  
pp. 159-170 ◽  
Author(s):  
E.J. Woltering ◽  
A. de Jong ◽  
F.A. Hoeberichts ◽  
E. Iakimova ◽  
V. Kapchina
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Flower Senescence
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