Regulation of Protein Degradation.

Callis, Judy

doi:10.1105/tpc.7.7.845

Cited by 209 publications

(70 citation statements)

References 92 publications

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“…Post-translational modifications (PTMs) are a common mechanism used to efficiently and rapidly regulate protein stability and degradation (Callis, 1995). To test if FEN1 degradation is PTM-mediated, we investigated the dynamics of FEN1 modifications during the cell cycle.…”

Section: Resultsmentioning

confidence: 99%

Sequential Posttranslational Modifications Program FEN1 Degradation during Cell-Cycle Progression

et al. 2012

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SUMMARY We propose that cell cycle-dependent timing of FEN1 nuclease activity is essential for cell cycle progression and the maintenance of genome stability. After DNA replication is complete at the exit point of the S-phase, removal of excess FEN1 may be crucial. Here, we report a mechanism that controls the programmed degradation of FEN1 via a sequential cascade of post-translational modifications. We found that FEN1 phosphorylation stimulated its SUMOylation, which, in turn, stimulated its ubiquitination and ultimately led to its degradation via the proteasome pathway. Mutations or inhibitors that blocked the modification at any step in this pathway suppressed FEN1 degradation. Critically, the presence of SUMOylation- or ubiquitination- defective, non-degradable FEN1 mutant protein caused accumulation of Cyclin B, delays in the G1 and G2/M phases and polyploidy. These findings may represent a newly identified regulatory mechanism used by cells to ensure precise cell cycle progression and to prevent transformation.

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Section: Resultsmentioning

confidence: 99%

Sequential Posttranslational Modifications Program FEN1 Degradation during Cell-Cycle Progression

et al. 2012

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“…As in other organisms, plant proteases are involved in a diverse array of processes (Vierstra 1993;Callis 1995). Nevertheless, and despite all the present lines of research, the restricted expression and high accumulation of a protease in stigmas has not, to the best of our knowledge, been reported until now.…”

Section: Discussionmentioning

confidence: 95%

Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L.

Ramalho-Santos

Pissarra

Verı́ssimo

et al. 1997

Planta

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The function of aspartic proteinases (EC 3.4.23) present in flowers of Cynara species is still unknown. Cardosin A, as a highly abundant aspartic proteinase from Cynara cardunculus L., a relative of the artichoke, is synthesised as a zymogen and subsequently undergoes proteolytic processing, yielding the mature and active enzyme. Here we report the study of the expression and localization of cardosin A, as a first approach to address the question of its physiological relevance. A polyclonal antibody specific for cardosin A was raised against a synthetic peptide corresponding to an amino acid sequence of the enzyme. This antibody was used to study the organ-specific, tissue-specific and subcellular localization of cardosin A by immunoblotting, tissue printing and immunogold electron microscopy. The results showed that expression of cardosin A is highly restricted to the pistils, and that the enzyme accumulates mainly in protein storage vacuoles of the stigmatic papillae. Cardosin A is also present, although much less abundantly, in the vacuoles of the cells of the epidermis of the style. In view of these results, the possible physiological roles of cardosin A are discussed, namely an involvement in defense mechanisms or pollen-pistil interaction, as well as in flower senescence.

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“…The addition of cysteine peptidases (CP) activator DTT (5 mM) or CPs irreversible inhibitor E-64 (5 mM) at pH 5 and pH 7 did not result in activity change (Table 1). These results exclude the presence of CPs [35] and indicate that the activity observed were exclusive of aspartyl-endopeptidases (AP). and stable between pH 2 and pH 10 was characterized in V. radiata [37].…”

Section: Peptidases Detected With Abz-aiaffsrq-eddnp Hydrolysismentioning

confidence: 85%

Proteolysis in the Subtropical Woody Tree <i>Anadenanthera colubrina</i> (Angico) Seeds during and after Germination

Barduche¹,

Livramento²,

Júdice³

et al. 2018

AJPS

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Proteolysis of seed storage proteins (SSP) during germination provides a steady supply of amino acids to the embryo development into seedling. This process is coordinated by different peptidases that act sequentially and overlaid mode. These enzymes are an ancient group evolved separately in a wide structural and functional diversity and have many applications in medicine, pharmacy and industry. However, the knowledge about seed peptidases during germination was obtained from studies almost restricted to the cultivated species. This restriction implies caution about generalizations made from these studies, as well limits the biological knowledge about plant kingdom and technological use from plant peptidases. In this work, a scan of the proteolytic activity was held in germinating seeds of a leguminous subtropical woody tree. Eleven proteolytic activities were detected in protein extracts from embryonic axis and cotyledons. The presence and intensity of these activities varied over time and between these tissues. There was indication that aspartyl-endopeptidases (phytepsins) and cysteine-carboxypeptidases (plant cathepsins) were involved in A. colubrina SSP hydrolysis. These peptidases differ to that commonly involved in germination of the cultivated leguminous. In addition, one of detected phytepsins showed stability on pH scale, which is important for industrial uses. There was also detected a metallo-carboxypeptidase activity, which has been not described in plants. These peptidases must be isolated to confirm or not these indications. However, these data indicate the biological and technological importance of extending the studies about plant peptidases on a diverse genetic basis.How to cite this paper: Barduche, D., do

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Regulation of Protein Degradation.

Cited by 209 publications

References 92 publications

Sequential Posttranslational Modifications Program FEN1 Degradation during Cell-Cycle Progression

Sequential Posttranslational Modifications Program FEN1 Degradation during Cell-Cycle Progression

Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L.

Proteolysis in the Subtropical Woody Tree <i>Anadenanthera colubrina</i> (Angico) Seeds during and after Germination

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Regulation of Protein Degradation.

Cited by 209 publications

References 92 publications

Sequential Posttranslational Modifications Program FEN1 Degradation during Cell-Cycle Progression

Sequential Posttranslational Modifications Program FEN1 Degradation during Cell-Cycle Progression

Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L.

Proteolysis in the Subtropical Woody Tree &lt;i&gt;Anadenanthera colubrina&lt;/i&gt; (Angico) Seeds during and after Germination

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Proteolysis in the Subtropical Woody Tree <i>Anadenanthera colubrina</i> (Angico) Seeds during and after Germination