Light-induced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.)

Planta ◽  
1986 ◽  
Vol 169 (2) ◽  
pp. 162-171 ◽  
Author(s):  
K. Dehesh ◽  
M. Klaas ◽  
I. H�user ◽  
K. Apel
Keyword(s):  
Hordeum Vulgare ◽  
Protochlorophyllide Oxidoreductase ◽  
Hordeum Vulgare L ◽  
Induced Changes ◽  
Cellular Compartments

Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression inEscherichia coli

1989 ◽  
Vol 217 (2-3) ◽  
pp. 355-361 ◽  
Author(s):  
Rüdiger Schulz ◽  
Klaus Steinmüller ◽  
Manfred Klaas ◽  
Christoph Forreiter ◽  
Sören Rasmussen ◽  
...  
Keyword(s):  
Hordeum Vulgare ◽  
Nucleotide Sequence ◽  
Inescherichia Coli ◽  
Protochlorophyllide Oxidoreductase ◽  
Hordeum Vulgare L ◽  
Expression Inescherichia Coli

Drought stress-induced changes in redox metabolism of barley (Hordeum vulgare L.)

2021 ◽  
Author(s):  
Ekumjot Kaur ◽  
Rachana D. Bhardwaj ◽  
Simarjit Kaur ◽  
Satvir K. Grewal
Keyword(s):  
Drought Stress ◽  
Hordeum Vulgare ◽  
Hordeum Vulgare L ◽  
Redox Metabolism ◽  
Induced Changes

scholarly journals Drought-induced changes in the actin cytoskeleton of barley (Hordeum vulgare L.) leaves

2015 ◽  
Vol 37 (4) ◽  
Author(s):  
Katarzyna Śniegowska-Świerk ◽  
Ewa Dubas ◽  
Marcin Rapacz
Keyword(s):  
Hordeum Vulgare ◽  
Actin Cytoskeleton ◽  
Hordeum Vulgare L ◽  
Induced Changes

scholarly journals Identification of the N-termini of NADPH : protochlorophyllide oxidoreductase A and B from barley etioplasts (Hordeum vulgare L.)

FEBS Journal ◽  
2009 ◽  
Vol 276 (4) ◽  
pp. 1074-1081 ◽  
Author(s):  
Matthias Plöscher ◽  
Bernhard Granvogl ◽  
Veronika Reisinger ◽  
Lutz A. Eichacker
Keyword(s):  
Hordeum Vulgare ◽  
Protochlorophyllide Oxidoreductase ◽  
Hordeum Vulgare L

Ultrastructure and Senescence in an Achloroplastic Mutant of Hordeum vulgare L. cv. Dyan

1992 ◽  
Vol 50 (1) ◽  
pp. 844-845
Author(s):  
R.H.M. Cross ◽  
C.E.J. Botha ◽  
A.K. Cowan ◽  
B.J. Hartley
Keyword(s):  
Cell Wall ◽  
Hordeum Vulgare ◽  
Leaf Tissue ◽  
Ultrastructural Changes ◽  
Hordeum Vulgare L ◽  
Mesophyll Cells ◽  
Lethal Mutant ◽  
Cytoplasmic Matrix ◽  
Close Proximity ◽  
Pinocytotic Vesicles

Senescence is an ordered degenerative process leading to death of individual cells, organs and organisms. The detection of a conditional lethal mutant (achloroplastic) of Hordeum vulgare has enabled us to investigate ultrastructural changes occurring in leaf tissue during foliar senescence.Examination of the tonoplast structure in six and 14 day-old mutant tissue revealed a progressive degeneration and disappearance of the membrane, apparently starting by day six in the vicinity of the mitochondria associated with the degenerating proplastid (Fig. 1.) where neither of the plastid membrane leaflets is evident (arrows, Fig. 1.). At this stage there was evidence that the mitochondrial membranes were undergoing retrogressive changes, coupled with disorganization of cristae (Fig. 2.). Proplastids (P) lack definitive prolamellar bodies. The cytoplasmic matrix is largely agranular, with few endoplasmic reticulum (ER) cisternae or polyribosomal aggregates. Interestingly, large numbers of actively-budding dictysomes, associated with pinocytotic vesicles, were observed in close proximity to the plasmalemma of mesophyll cells (Fig. 3.). By day 14 however, mesophyll cells showed almost complete breakdown of subcellular organelle structure (Fig. 4.), and further evidence for the breakdown of the tonoplast. The final stage of senescence is characterized by the solubilization of the cell wall due to expression and activity of polygalacturonase and/or cellulose. The presence of dictyosomes with associated pinocytotic vesicles formed from the mature face, in close proximity to both the plasmalemma and the cell wall, would appear to support the model proposed by Christopherson for the secretion of cellulase. This pathway of synthesis is typical for secretory glycoproteins.

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