scholarly journals Protein Degradation Rate in Arabidopsis thaliana Leaf Growth and Development

2017 ◽  
Vol 29 (2) ◽  
pp. 207-228 ◽  
Author(s):  
Lei Li ◽  
Clark J. Nelson ◽  
Josua Trösch ◽  
Ian Castleden ◽  
Shaobai Huang ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein Degradation ◽  
Growth And Development ◽  
Degradation Rate ◽  
Leaf Growth ◽  
Protein Degradation Rate

Impact of Weighing Procedures and Variation in Protein Degradation Rate on Measured Performance of Growing Lambs and Cattle

1983 ◽  
Vol 57 (5) ◽  
pp. 1276-1285 ◽  
Author(s):  
Rick Stock ◽  
Terry Klopfenstein ◽  
Dennis Brink ◽  
Steve Lowry ◽  
Dave Rock ◽  
...  
Keyword(s):  
Protein Degradation ◽  
Degradation Rate ◽  
Protein Degradation Rate

Overexpression of Akt2 in Oral Cancer Cells is Due To Reduced Protein Degradation Rate

2015 ◽  
Vol 119 (3) ◽  
pp. e108
Author(s):  
Anak Iamaroon ◽  
Supansa Pata ◽  
Prakasit Archewa ◽  
Chayarop Supanachart ◽  
Sutthichai Krisanaprakornkit
Keyword(s):  
Oral Cancer ◽  
Protein Degradation ◽  
Cancer Cells ◽  
Degradation Rate ◽  
Oral Cancer Cells ◽  
Protein Degradation Rate

In vitro ruminal undegradable proteins of alfalfa cultivars

2000 ◽  
Vol 80 (2) ◽  
pp. 315-325 ◽  
Author(s):  
G. F. Tremblay ◽  
R. Michaud ◽  
G. Bélanger ◽  
K. B. McRae ◽  
H. V. Petit
Keyword(s):  
Protein Degradation ◽  
Dry Matter ◽  
Degradation Rate ◽  
Weight Ratio ◽  
Principal Component ◽  
Neutral Detergent Fiber ◽  
Cultivar Differences ◽  
Dry Matter Digestibility ◽  
Protein Degradation Rate

The quality of alfalfa would be greatly improved by an increase in its ruminal undegradable protein (RUP) concentration. Protein degradation rate (PDR), in vitro dry matter digestibility (IVDMD), leaf weight ratio (LWR), dry matter yield (DMY), total nitrogen (TN), in vitro RUP (expressed on both TN, RUP-TN, and dry matter basis, RUP-DM), acid detergent fiber (ADF), and neutral detergent fiber (NDF) concentrations were determined in 27 alfalfa cultivars. Cultivars were seeded in triplicate on 2 consecutive years and evaluated during the 2 subsequent production years with two harvests per year. Protein degradation rate and RUP-TN were determined using a ruminal inhibitor in vitro system. Data were averaged for spring growth, summer regrowth, and both harvests across 2 production years. Each of the three data sets was analyzed by ANOVA followed by a principal component analysis (PCA) on the ANOVA means. For the four-harvest data, cultivar differences were highly significant (P < 0.001) for all variates except for PDR (P = 0.07) and RUP-TN concentration (P = 0.10). The first PCA axis was largely defined positively by RUP-DM, IVDMD, TN, LWR, and RUP-TN, but negatively with ADF, NDF, PDR, and DMY. The second PCA axis defined a contrast between PDR versus RUP-TN, DMY, ADF, and NDF. Five cultivars were distinctive with high or low PCA scores in all three PCA. Rangelander and Heinrichs, along with Ultra, had low PDR; the first two cultivars had low DMY whereas Ultra was a medium-yielding cultivar. In contrast, Algonquin and Oneida VR had high PDR and medium DMY. While the first principal component (PC) indicated a general trend that low PDR and high RUP were associated with low-yielding cultivars, the second PC identified specific cultivars with both low PDR and high DMY. Therefore, selection for low PDR and high DMY is feasible. Key words: ruminal protein escape, dry matter digestibility, alfalfa

Dependence of the period on the rate of protein degradation in minimal models for circadian oscillations

2009 ◽  
Vol 367 (1908) ◽  
pp. 4665-4683 ◽  
Author(s):  
Claude Gérard ◽  
Didier Gonze ◽  
Albert Goldbeter
Keyword(s):  
Circadian Rhythms ◽  
Protein Degradation ◽  
Degradation Rate ◽  
Protein Product ◽  
Degree Of Saturation ◽  
Minimal Models ◽  
Biochemical Processes ◽  
Parameter Values ◽  
Protein Degradation Rate ◽  
Clock Protein

Circadian rhythms, which occur spontaneously with a period of about 24 h in a variety of organisms, allow their adaptation to the periodic variations of the environment. These rhythms are generated by a genetic regulatory network involving a negative feedback loop on transcription. Mathematical models based on the negative autoregulation of gene expression by the protein product of a clock gene account for the occurrence of self-sustained circadian oscillations. These models differ by their degree of complexity and, hence, by the number of variables considered. Some of these models can be considered as minimal because they contain a reduced number of biochemical processes and variables capable of producing sustained oscillations. In three of these minimal models, the period of the oscillations significantly changes with the rate of degradation of the clock protein. However, depending on the model considered, the period increases, decreases or passes through a maximum as a function of the protein degradation rate. We clarify the bases for these markedly different results by bringing to light the roles of (i) protein phosphorylation, which is required for protein degradation, and (ii) the velocity and degree of saturation of mRNA and protein degradation. Changes in the parameter values of the more complex of the minimal models can produce the period profiles observed in the other two models. The analysis allows us to reconcile the contradictory predictions for the dependence of the period on the clock protein degradation rate in three minimal models used to describe circadian rhythms.

scholarly journals PAQR9 Modulates BAG6-mediated protein quality control of mislocalized membrane proteins

2020 ◽  
Vol 477 (2) ◽  
pp. 477-489
Author(s):  
Xue You ◽  
Yijun Lin ◽  
Yongfan Hou ◽  
Lijiao Xu ◽  
Qianqian Cao ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Quality Control ◽  
Membrane Proteins ◽  
Protein Degradation ◽  
Degradation Rate ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Dependent Manner ◽  
Cellular Homeostasis ◽  
Protein Degradation Rate

Protein quality control is crucial for maintaining cellular homeostasis and its dysfunction is closely linked to human diseases. The post-translational protein quality control machinery mainly composed of BCL-2-associated athanogene 6 (BAG6) is responsible for triage of mislocalized membrane proteins (MLPs). However, it is unknown how the BAG6-mediated degradation of MLPs is regulated. We report here that PAQR9, a member of the Progesterone and AdipoQ receptor (PAQR) family, is able to modulate BAG6-mediated triage of MLPs. Analysis with mass spectrometry identified that BAG6 is one of the major proteins interacting with PAQR9 and such interaction is confirmed by co-immunoprecipitation and co-localization assays. The protein degradation rate of representative MLPs is accelerated by PAQR9 knockdown. Consistently, the polyubiquitination of MLPs is enhanced by PAQR9 knockdown. PAQR9 binds to the DUF3538 domain within the proline-rich stretch of BAG6. PAQR9 reduces the binding of MLPs to BAG6 in a DUF3538 domain-dependent manner. Taken together, our results indicate that PAQR9 plays a role in the regulation of protein quality control of MLPs via affecting the interaction of BAG6 with membrane proteins.

scholarly journals Recent advances in measuring and understanding the regulation of exercise-mediated protein degradation in skeletal muscle

2021 ◽  
Author(s):  
Yusuke Nishimura ◽  
Ibrahim Musa ◽  
Lars Holm ◽  
Yu-Chiang Lai
Keyword(s):  
Skeletal Muscle ◽  
Quality Control ◽  
Protein Degradation ◽  
Protein Turnover ◽  
Degradation Rate ◽  
Protein Quality ◽  
Muscle Protein ◽  
Protein Quality Control ◽  
Muscle Protein Degradation ◽  
Protein Degradation Rate

Skeletal muscle protein turnover plays a crucial role in controlling muscle mass and protein quality control, including sarcomeric (structural and contractile) proteins. Protein turnover is a dynamic and continual process of protein synthesis and degradation. The ubiquitin proteasome system (UPS) is a key degradative system for protein degradation and protein quality control in skeletal muscle. UPS-mediated protein quality control is known to be impaired in ageing and diseases. Exercise is a well-recognized non-pharmacological approach to promote muscle protein turnover rates. Over the past decades, we have acquired substantial knowledge of molecular mechanisms of muscle protein synthesis after exercise. However, there has been considerable gaps in the mechanisms of how muscle protein degradation is regulated at the molecular level. The main challenge to understand muscle protein degradation is due in part to the lack of solid stable isotope tracer methodology to measure muscle protein degradation rate. Understanding the mechanisms of UPS with the concomitant measurement of protein degradation rate in skeletal muscle will help identify novel therapeutic strategies to ameliorate impaired protein turnover and protein quality control in ageing and diseases. Thus, the goal of this present review is to highlight how recent advances in the field may help improve our understanding of exercise-mediated protein degradation. We discuss 1) the emerging roles of protein phosphorylation and ubiquitylation modifications in regulating proteasome-mediated protein degradation after exercise and 2) methodological advances to measure in vivo myofibrillar protein degradation rate using stable isotope tracer methods.

scholarly journals Defects in autophagy lead to selective in vivo changes in turnover of cytosolic and organelle proteins in Arabidopsis

2021 ◽  
Author(s):  
Lei Li ◽  
Chun Pong Lee ◽  
Akila Wijerathna-Yapa ◽  
Martyna Broda ◽  
Marisa S. Otegui ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Degradation Rate ◽  
T Complex ◽  
Autophagy Induction ◽  
Degradation Rates ◽  
Specific Proteins ◽  
Protein Degradation Rate ◽  
Synthesis And Degradation

AbstractIdentification of autophagic protein cargo in plants by their abundance in autophagy related genes (ATG) mutants is complicated by changes in both protein synthesis and protein degradation. To detect autophagic cargo, we measured protein degradation rate in shoots and roots of Arabidopsis atg5 and atg11 mutant plants. These data show that less than a quarter of proteins changing in abundance are probable cargo and revealed roles of ATG11 and ATG5 in degradation of specific cytosol, chloroplast and ER-resident proteins, and a specialized role for ATG11 in degradation of proteins from mitochondria and chloroplasts. Our data support a role for autophagy in degrading glycolytic enzymes and the chaperonin containing T-complex polypeptide-1 complex. Autophagy induction by Pi limitation changed metabolic profiles and the protein synthesis and degradation rates of atg5 and atg11 plants. A general decrease in the abundance of amino acids and increase in several secondary metabolites in autophagy mutants was consistent with altered catabolism and changes in energy conversion caused by reduced degradation rate of specific proteins. Combining measures of changes in protein abundance and degradation rates, we also identify ATG11 and ATG5 associated protein cargo of low Pi induced autophagy in chloroplasts and ER-resident proteins involved in secondary metabolism.Single Sentence SummaryProtein cargo of autophagy in plants can be discovered by identifying proteins that increase in abundance and decrease in degradation rate in mutants deficient in autophagy machinery

scholarly journals Timescale of degradation-driven protein level fluctuation in the yeast Saccharomyces cerevisiae

2021 ◽  
Author(s):  
Bahareh Mahrou ◽  
Azady Pirhanov ◽  
Moluk Hadi Alijanvand ◽  
Yong Ku Cho ◽  
Yong-Jun Shin
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Degradation ◽  
Protein Level ◽  
Transcriptional Control ◽  
Degradation Rate ◽  
Modulation Frequency ◽  
Cellular Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Protein Levels ◽  
Protein Degradation Rate

Generating robust, predictable perturbations in cellular protein levels will advance our understanding of protein function and enable control of physiological outcomes in biotechnology applications. Previous studies have shown that controlling RNA transcription achieves perturbations in protein levels over a timescale of several hours. Here, we demonstrate the potential for harnessing the protein degradation machinery to achieve robust, rapid control of a specific protein level in the yeast Saccharomyces cerevisiae. Using a light-driven protein degradation machinery and red fluorescent proteins as reporters, we show that under constant transcriptional induction, repeated triangular fluctuations in protein levels can be generated by controlling the protein degradation rate. Consistent with previous results using transcriptional control, we observed a continuous decrease in the magnitude of fluctuations as the modulation frequency increased, indicating low-pass filtering of input perturbation. However, compared to hour-scale fluctuations observed using transcriptional control, modulating the protein degradation rate enabled five to ten minute-scale fluctuations. Our study demonstrates the potential for repeated control of protein levels by controlling protein degradation rate, at timescales much shorter than that achieved by transcriptional control.

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