Partial Reversal of Temperature‐dependent Inhibition of Soybean Hypocotyl Elongation by Cotyledon Excision 1

Crop Science ◽  
1975 ◽  
Vol 15 (4) ◽  
pp. 461-462 ◽  
Author(s):  
J. S. Burris ◽  
K. H. Knittle
2013 ◽  
Vol 67 (2) ◽  
pp. 392-401 ◽  
Author(s):  
Beck R. Frydenborg ◽  
Cory J. Krediet ◽  
Max Teplitski ◽  
Kim B. Ritchie

2002 ◽  
Vol 48 (9) ◽  
pp. 821-830 ◽  
Author(s):  
Ann M Gustafson ◽  
Kevin P O'Connell ◽  
Michael F Thomashow

We previously reported that mutants of Sinorhizobium meliloti 1021 carrying luxAB insertions in each of the three 16S rRNA genes exhibited a dramatic ([Formula: see text]28-fold) increase in luminescence following a temperature downshift from 30 to 15°C. These results raised the possibility that the rRNA operons (rrn) of S. meliloti were cold shock loci. In testing this possibility, we found that fusion of the S. meliloti 1021 rrnA promoter to two different reporter genes, luxAB and uidA, resulted in hybrid genes that were transiently upregulated (as measured by transcript accumulation) about four- to sixfold in response to a temperature downshift. These results are consistent with the hypothesis that the rrn promoters are transiently upregulated in response to cold shock. However, much of the apparent cold shock regulation of the initial luxAB insertions was due to an unexpected mechanism: an apparent temperature-dependent inhibition of translation. Specifically, the rrnA sequences from +1 to +172 (relative to the start of transcription) were found to greatly decrease the ability of S. meliloti to translate hybrid rrn–luxAB transcripts into active protein at 30°C. This effect, however, was largely eliminated at 15°C. Possible mechanisms for the apparent transient increase in rrnA promoter activity and temperature-dependent inhibition of translation are discussed.Key words: rhizobium, gene expression, luciferase.


Blood ◽  
1986 ◽  
Vol 68 (1) ◽  
pp. 239-243 ◽  
Author(s):  
R Weiss ◽  
M Silverberg ◽  
AP Kaplan

Using components purified from human plasma, we have examined the effects of C1 inhibitor (C1 INH), the primary inhibitor of activated Hageman Factor (HFa) and Hageman factor fragment (HFf), on Hageman Factor (HF) autoactivation. When Hageman factor was exposed to a negatively charged surface, provided by either a glass cuvette or dextran sulfate, the addition of C1 INH gave a dose-dependent inhibition of the activity observed. The ability of C1 INH to decrease the maximal enzymatic activity generated was markedly temperature dependent with inhibition increasing as the temperature was raised from 4 degrees C to 37 degrees C. Although the rates of both autoactivation and inhibition were decreased at lower temperatures (4 degrees C), the latter rate was more sensitive to temperature modulation. When HF (final concentration 1 mumol/L) was incubated with C1 INH (0.54, 1.07, and 2.14 mumol/L) in the absence of an initiating surface, no increases in enzymatic activity were observed for up to 48 hours regardless of the C1 INH concentration. However, SDS polyacrylamide gel electrophoresis of the incubation mixture revealed that HF autodigestion had occurred by 48 hours despite the presence of C1 INH. In addition, the appearance of a new band suggested that a complex had been formed between the inhibitor and activated HF. Our findings indicate that C1 INH does not prevent HF autoactivation but rather inactivates the products of HF autodigestion.


1972 ◽  
Vol 10 (1) ◽  
pp. 159-161 ◽  
Author(s):  
William R. Gallaher ◽  
Michael A. Bratt

Blood ◽  
1986 ◽  
Vol 68 (1) ◽  
pp. 239-243 ◽  
Author(s):  
R Weiss ◽  
M Silverberg ◽  
AP Kaplan

Abstract Using components purified from human plasma, we have examined the effects of C1 inhibitor (C1 INH), the primary inhibitor of activated Hageman Factor (HFa) and Hageman factor fragment (HFf), on Hageman Factor (HF) autoactivation. When Hageman factor was exposed to a negatively charged surface, provided by either a glass cuvette or dextran sulfate, the addition of C1 INH gave a dose-dependent inhibition of the activity observed. The ability of C1 INH to decrease the maximal enzymatic activity generated was markedly temperature dependent with inhibition increasing as the temperature was raised from 4 degrees C to 37 degrees C. Although the rates of both autoactivation and inhibition were decreased at lower temperatures (4 degrees C), the latter rate was more sensitive to temperature modulation. When HF (final concentration 1 mumol/L) was incubated with C1 INH (0.54, 1.07, and 2.14 mumol/L) in the absence of an initiating surface, no increases in enzymatic activity were observed for up to 48 hours regardless of the C1 INH concentration. However, SDS polyacrylamide gel electrophoresis of the incubation mixture revealed that HF autodigestion had occurred by 48 hours despite the presence of C1 INH. In addition, the appearance of a new band suggested that a complex had been formed between the inhibitor and activated HF. Our findings indicate that C1 INH does not prevent HF autoactivation but rather inactivates the products of HF autodigestion.


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