Cytoplasmic regulation of translation during Ilyanassa embryogenesis

Development ◽  
1989 ◽  
Vol 106 (2) ◽  
pp. 263-269
Author(s):  
Collier JR
Keyword(s):  
Protein Synthesis ◽  
Actinomycin D ◽  
Specific Gene ◽  
Early Cleavage ◽  
Polar Lobe ◽  
Nuclear Activity ◽  
Two Dimensional Electrophoresis ◽  
Regulation Of Translation ◽  
Maternal Mrnas ◽  
Dimensional Electrophoresis

Two-dimensional electrophoresis of labeled proteins and hybridization of mRNAs with specific gene probes was demonstrate changes in protein synthesis, and the of actin maternal mRNAs during the early development isolated polar lobe was used as a nucleus-free egg the regulation of translation. It was shown that actin present in the unfertilized egg and are therefore are inactive during early cleavage, and are translated lobeless, actinomycin D-treated blastulae and in that have been aged for 24h. Thus, the activation of controlled by cytoplasmic factors that function cleavage and nuclear activity. I suggest that the cytoplasmic clock determines when maternal mRNAs are that this clock is made and set running during protein synthesis that occurred during early cleavage also involve the diminution of some early cleavage suggested that this diminution is controlled by localized in the blastomeres of the lobeless egg but polar lobe.

Polyribosome fractions and protein synthesis in stem rust infected wheat

1986 ◽  
Vol 64 (9) ◽  
pp. 1916-1927 ◽  
Author(s):  
Andrew Greenland ◽  
Michael Shaw
Keyword(s):  
Protein Synthesis ◽  
Stem Rust ◽  
Rust Fungus ◽  
High Molecular Mass ◽  
In Vitro Translation ◽  
Ribosomal Subunits ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

The effects of infection by stem-rust fungus on polyribosomal RNA fractions and protein synthesis in vitro and in vivo in near-isogenic resistant (Sr6) and susceptible (sr6) lines of wheat were determined. In infected resistant leaves the proportion of ribosomes present as polyribosomes was greater than that in healthy (uninfected) leaves at 1, 3, and 6 days and that in susceptible leaves at 1 and 3 days after inoculation. In the latter there were large increases in the pelletable RNA content (ribosomes, ribosomal subunits, and polyribosomes) and proportion of ribosomes present as polyribosomes from day 6. In vitro translation failed to detect any marked differences in polyribosomal translation products in resistant and susceptible leaves in response to infection. Labelling of polypeptides in vivo and separation by one- and two-dimensional electrophoresis showed that at 1 day after inoculation, two groups of high molecular mass polypeptides (80–96 and 100–110 kDa) were more heavily labelled and two novel polypeptides were present in resistant and susceptible leaves in response to infection. Synthesis of the high molecular weight and two novel polypeptides was maintained in infected resistant leaves up to 6 days after inoculation. In susceptible leaves the amount of radiolabel incorporated into these polypeptides and several proteins prominently labelled in uninfected controls declined rapidly from 3 days after inoculation.

Protein synthesis in flax following inoculation with flax rust

1986 ◽  
Vol 64 (1) ◽  
pp. 13-18 ◽  
Author(s):  
Ben C. S. Sutton ◽  
Michael Shaw
Keyword(s):  
Protein Synthesis ◽  
Large Subunit ◽  
Two Dimensional ◽  
Bisphosphate Carboxylase ◽  
Two Dimensional Electrophoresis ◽  
Host Pathogen Interaction ◽  
Melampsora Lini ◽  
In Vivo Labelling ◽  
Dimensional Electrophoresis

Resistance to flax rust Melampsora lini (Ehrenb.) Lév. in flax carrying the N resistance gene is determined by 24 h postinoculation, at which time hypersensitivity is observed. We have examined protein synthesis in cotyledons inoculated with both virulent and avirulent races of rust by in vivo labelling with [35S]methionine. The pattern of protein synthesis was assessed by one- and two-dimensional electrophoresis 8, 13, and 18 h after inoculation. No changes in protein synthesis were observed in the first 14 h following inoculation; however, by 18 h after inoculation the susceptible combination showed a marked decrease in protein synthesis (22%; P = 0.01). This could be largely accounted for by the reduced synthesis of the ribulose 1,5-bisphosphate carboxylase large subunit, which was readily quantified on electrophoresis gels. In addition, a 30-kDa polypeptide also declined in the susceptible combination. Two-dimensional electrophoresis enabled changes to be detected in the synthesis of other minor polypeptides. None of these changes were observed in the resistant combination in which a small increase in the synthesis of the ribulose 1,5-bisphosphate carboxylase large subunit and the 30-kDa polypeptide was found. These results indicate that the outcome of the host–pathogen interaction has already been determined by 18 h after inoculation.

Sialic Acid Dependent Polypeptide Chain Heterogeneity of Human Fibrinogen Demonstrated by Two-Dimensional Electrophoresis

1982 ◽  
Vol 47 (01) ◽  
pp. 019-021 ◽  
Author(s):  
Cemal Kuyas ◽  
André Haeberli ◽  
P Werner Straub
Keyword(s):  
Sialic Acid ◽  
Polypeptide Chain ◽  
Two Dimensional ◽  
Charge Heterogeneity ◽  
Human Fibrinogen ◽  
Two Dimensional Electrophoresis ◽  
Isoelectric Points ◽  
Polypeptide Chains ◽  
Dimensional Electrophoresis ◽  
Chain Type

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.

EFFECT OF ACTINOMYCIN D ON TSH-INDUCED STIMULATION OF THYROIDAL PROTEIN SYNTHESIS IN THE RAT

1974 ◽  
Vol 77 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Gustav Wägar
Keyword(s):  
Protein Synthesis ◽  
Actinomycin D ◽  
The Other ◽  
Leucine Incorporation ◽  
Short Term ◽  
Other Hand ◽  
Thyroid Glands ◽  
Translational Level ◽  
Stimulation Of

ABSTRACT Whether the short-term regulation of thyroidal protein synthesis by TSH occurs at the transcriptional or the translational level was tested by measuring the effect of actinomycin D (act D) on the TSH-induced stimulation of L-14C-leucine incorporation into the thyroidal proteins of rats. TSH was injected 6 h before the rats were killed. The thyroid glands were then removed and incubated in vitro in the presence of L-14C-leucine for 2 h. The pronounced stimulation of leucine incorporation in the TSH-treated animals was depressed as compared with controls but still significant even when the animals had been pre-treated with 100 μg act D 24 and 7 h before sacrifice. On the other hand, act D strongly decreased incorporation of 3H-uridine into RNA. Short-term regulation of thyroidal protein synthesis by TSH appears to be partly but not wholly dependent on neosynthesis of RNA. Hence regulation may partly occur at the translation level of protein synthesis.

Improvement of Two-dimensional Electrophoresis of Rice (Oryza sativaL.) Proteomics

2012 ◽  
Vol 18 (5) ◽  
pp. 819 ◽  
Author(s):  
Yanhua YANG ◽  
Weitong CUI ◽  
Xiaoyong LIU ◽  
Keming ZHU ◽  
Keping CHEN
Keyword(s):  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis
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