Autoradiographic study of the effect of 5-aminouracil on the S phase and mitosis of barley root meristems

1979 ◽  
Vol 21 (3) ◽  
pp. 187-192 ◽  
Author(s):  
M. Ondřej ◽  
Květuše Schwammenhöferová
2002 ◽  
Vol 77 (3) ◽  
pp. 145-152 ◽  
Author(s):  
J. P. Hervás ◽  
J. de la Flor ◽  
M. C. Santa-Cruz
Keyword(s):  
S Phase ◽  

1987 ◽  
Vol 71 (1) ◽  
pp. 68-72 ◽  
Author(s):  
Marisa Levi ◽  
Elio Sparvoli ◽  
Sergio Sgorbati ◽  
Donato Chiatante
Keyword(s):  
S Phase ◽  

1983 ◽  
Vol 25 (4) ◽  
pp. 288-292
Author(s):  
Blanka Vostřáková-Němcová ◽  
S. Rakouský ◽  
M. Ondřej
Keyword(s):  

2002 ◽  
Vol 77 (3) ◽  
pp. 145-152 ◽  
Author(s):  
J P Hervás ◽  
J de la Flor ◽  
M C Santa-Cruz
Keyword(s):  
S Phase ◽  

2021 ◽  
Vol 12 ◽  
Author(s):  
Federico Martinez-Seidel ◽  
Pipob Suwanchaikasem ◽  
Shuai Nie ◽  
Michael G. Leeming ◽  
Alexandre Augusto Pereira Firmino ◽  
...  

Due to their sessile nature, plants rely on root systems to mediate many biotic and abiotic cues. To overcome these challenges, the root proteome is shaped to specific responses. Proteome-wide reprogramming events are magnified in meristems due to their active protein production. Using meristems as a test system, here, we study the major rewiring that plants undergo during cold acclimation. We performed tandem mass tag-based bottom-up quantitative proteomics of two consecutive segments of barley seminal root apexes subjected to suboptimal temperatures. After comparing changes in total and ribosomal protein (RP) fraction-enriched contents with shifts in individual protein abundances, we report ribosome accumulation accompanied by an intricate translational reprogramming in the distal apex zone. Reprogramming ranges from increases in ribosome biogenesis to protein folding factors and suggests roles for cold-specific RP paralogs. Ribosome biogenesis is the largest cellular investment; thus, the vast accumulation of ribosomes and specific translation-related proteins during cold acclimation could imply a divergent ribosomal population that would lead to a proteome shift across the root. Consequently, beyond the translational reprogramming, we report a proteome rewiring. First, triggered protein accumulation includes spliceosome activity in the root tip and a ubiquitous upregulation of glutathione production and S-glutathionylation (S-GSH) assemblage machineries in both root zones. Second, triggered protein depletion includes intrinsically enriched proteins in the tip-adjacent zone, which comprise the plant immune system. In summary, ribosome and translation-related protein accumulation happens concomitantly to a proteome reprogramming in barley root meristems during cold acclimation. The cold-accumulated proteome is functionally implicated in feedbacking transcript to protein translation at both ends and could guide cold acclimation.


1983 ◽  
Vol 60 (1) ◽  
pp. 51-65
Author(s):  
M. Fujishima

Timing and duration of pre-meiotic G1, S and G2 phases in Paramecium caudatum have been clarified by microspectrophotometry of DNA content and autoradiography with [3H]thymidine ([3H]dThd) and [3H]deoxyuridinemonophosphate ([3H]dUMP). Microspectrophotometric measurement of DNA content showed that cells in stationary phase have a G1 micronucleus, and that pre-meiotic DNA synthesis begins with the micronuclear swelling and ends immediately before the nucleus enters meiotic prophase. The results indicate that the micronucleus is in G1 during the first 1.5 h after onset of mating reaction at 25 degrees C and in pre-meiotic S phase during the following 1 h, and that G2 phase is very short or lacking. Therefore, in P. caudatum, the transition point from pre-meiotic interphase to meiotic prophase is at or very close to the end of pre-meiotic DNA synthesis. Autoradiographic study showed that although [3H]dThd and [3H]dUMP were well utilized in pre-mitotic DNA synthesis, only [3H]dUMP was well utilized in pre-meiotic DNA synthesis. [3H]dThd was utilized very little in pre-meiotic DNA synthesis even if the precursor was taken into the cell, suggesting that the activity of thymidine kinase is low in these cells.


Sign in / Sign up

Export Citation Format

Share Document