Ribosomal Slowdown Mediates Translational Arrest during Cellular Division

Sivan, Gilad; Kedersha, Nancy; Elroy‐Stein, Orna

doi:10.1128/mcb.00798-07

Cited by 108 publications

(117 citation statements)

References 35 publications

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“…It is suggested that the highly sulfated chitosan mainly affected the intrinsic pathway, and has little effect on the assays reflecting extrinsic pathway. The results of the present study were dissimilar on Scanthophagus argus venom also not shown any disturbance in the plasma clotting time [22]. But, similar to protease from Vipera labetina [23], Naja naja [24], Naja melanolenca, Naja pallid, Crotalus argus atrox venom prolonged the coagulation of citrated plasma and shown the anticoagulant activity [25].…”

Section: Anticoagulant Activitymentioning

confidence: 96%

RETRACTED ARTICLE: Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

et al. 2015

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This study is designed to isolate and purify a novel anti-clotting protein component from the venom of Enhydrina schistosa, and explore its biochemical and biological activities. The active protein was purified from the venom of E. schistosa by ion-exchange chromatography using DEAE-cellulose. The venom protein was tested by various parameters such as, proteolytic, haemolytic, phospholipase and anti-coagulant activities. 80 % purity was obtained in the final stage of purification and the purity level of venom was revealed as a single protein band of about 44 kDa in SDS-polyacrylamide electrophoresis under reducing conditions. The results showed that the Potent hemolytic activity was observed against cow, goat, chicken and human (A, B and O positive) erythrocytes. Furthermore, the clotting assays showed that the venom of E. schistosa significantly prolonged in activated partial thromboplastin time, thrombin time, and prothrombin time. Venomous enzymes which hydrolyzed casein and gelatin substrate were found in this venom protein. Gelatinolytic activity was optimal at pH 5-9 and 1 H NMR analysis of purified venom was the base line information for the structural determination. These results suggested that the E. schistosa venom holds good promise for the development of novel lead compounds for pharmacological applications in near future.

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Section: Anticoagulant Activitymentioning

confidence: 96%

RETRACTED ARTICLE: Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

et al. 2015

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“…The approaches used differed both in terms of obtaining mitotic cells (release from aphidicolin-or thymidine-induced S-phase block versus mitotic shake-off) and the procedure used to study eEF2 phosphorylation (analysis with a phospho-specific antibody versus 2D gel electrophoresis, as the phosphorylation site in eEF2 (Thr56) had not been identified at that time). While this paper was under review, it was reported (Sivan et al, 2007) that eEF2 phosphorylation was elevated in cells in M-phase, although it was not explained how the synthesis of specific polypeptides could continue in mitotic cells if elongation is inhibited. Our data do provide an explanation for this, by showing that eEF2 is unphosphorylated in mitotic cells.…”

Section: Discussionmentioning

confidence: 99%

cdc2–cyclin B regulates eEF2 kinase activity in a cell cycle- and amino acid-dependent manner

Smith

Proud

2008

EMBO J

101

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The calcium/calmodulin‐dependent kinase that phosphorylates and inactivates eukaryotic elongation factor 2 (eEF2 kinase; eEF2K) is subject to multisite phosphorylation, which regulates its activity. Phosphorylation at Ser359 inhibits eEF2K activity even at high calcium concentrations. To identify the kinase that phosphorylates Ser359 in eEF2K, we developed an extensive purification protocol. Tryptic mass fingerprint analysis identified it as cdc2 (cyclin‐dependent kinase 1). cdc2 co‐purifies with Ser359 kinase activity and cdc2–cyclin B complexes phosphorylate eEF2K at Ser359. We demonstrate that cdc2 contributes to controlling eEF2 phosphorylation in cells. cdc2 is activated early in mitosis. Kinase activity against Ser359 in eEF2K also peaks at this stage of the cell cycle and eEF2 phosphorylation is low in mitotic cells. Inactivation of eEF2K by cdc2 may serve to keep eEF2 active during mitosis (where calcium levels rise) and thereby permit protein synthesis to proceed in mitotic cells. Amino‐acid starvation decreases cdc2's activity against eEF2K, whereas loss of TSC2 (a negative regulator of mammalian target of rapamycin complex 1(mTORC1)) increases it. These data closely match the control of Ser359 phosphorylation and indicate that cdc2 may be regulated by mTORC1.

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“…However, slower elongation rates have been associated with the accumulation of heavier polysomes both in yeast and mammals (Hovland et al, 1999;Shenton et al, 2006;Sivan et al, 2007). As a result, mRNAs densely covered with ribosomes might be protected from degradation by nucleases, becoming more stable (Deana and Belasco, 2005;Dreyfus, 2009).…”

Section: The Absence Of Cp-trna Arg (Icg) Slows Down Chloroplast Tranmentioning

confidence: 99%

Arabidopsis tRNA Adenosine Deaminase Arginine Edits the Wobble Nucleotide of Chloroplast tRNAArg(ACG) and Is Essential for Efficient Chloroplast Translation

et al. 2009

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RNA editing changes the coding/decoding information relayed by transcripts via nucleotide insertion, deletion, or conversion. Editing of tRNA anticodons by deamination of adenine to inosine is used both by eukaryotes and prokaryotes to expand the decoding capacity of individual tRNAs. This limits the number of tRNA species required for codon-anticodon recognition. We have identified the Arabidopsis thaliana gene that codes for tRNA adenosine deaminase arginine (TADA), a chloroplast tRNA editing protein specifically required for deamination of chloroplast (cp)-tRNA Arg (ACG) to cp-tRNA Arg (ICG). Land plant TADAs have a C-terminal domain similar in sequence and predicted structure to prokaryotic tRNA deaminases and also have very long N-terminal extensions of unknown origin and function. Biochemical and mutant complementation studies showed that the C-terminal domain is sufficient for cognate tRNA deamination both in vitro and in planta. Disruption of TADA has profound effects on chloroplast translation efficiency, leading to reduced yields of chloroplast-encoded proteins and impaired photosynthetic function. By contrast, chloroplast transcripts accumulate to levels significantly above those of wild-type plants. Nevertheless, absence of cp-tRNA Arg (ICG) is compatible with plant survival, implying that two out of three CGN codon recognition occurs in chloroplasts, though this mechanism is less efficient than wobble pairing.

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Ribosomal Slowdown Mediates Translational Arrest during Cellular Division

Cited by 108 publications

References 35 publications

RETRACTED ARTICLE: Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

RETRACTED ARTICLE: Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

cdc2–cyclin B regulates eEF2 kinase activity in a cell cycle- and amino acid-dependent manner

Arabidopsis tRNA Adenosine Deaminase Arginine Edits the Wobble Nucleotide of Chloroplast tRNAArg(ACG) and Is Essential for Efficient Chloroplast Translation

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