scholarly journals Expression profile of protein fractions in the developing kernel of normal, Opaque-2 and quality protein maize

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Mehak Sethi ◽  
Alla Singh ◽  
Harmanjot Kaur ◽  
Ramesh Kumar Phagna ◽  
Sujay Rakshit ◽  
...  
Keyword(s):  
Protein Quality ◽  
Immature Stage ◽  
Protein Fractions ◽  
Quality Protein Maize ◽  
Agronomic Performance ◽  
Kernel Development ◽  
Hard Kernel ◽  
Maize Varieties ◽  
Maize Protein

AbstractMaize protein quality is determined by the composition of its endosperm proteins, which are classified as nutritionally poor zeins (prolamin and prolamin-like) and nutritionally rich non-zeins (albumin, globulin, glutelin-like, and glutelin). Protein quality is considerably higher in opaque-2 mutants due to increased content of non-zeins over zeins. However, the opaque-2 endosperm is soft, which leads to poor agronomic performance and post-harvest infestation. Endosperm modification of opaque-2 had led to the development of Quality Protein Maize (QPM), which has higher protein quality along with hard kernel endosperm. The present study was planned to analyze the expression dynamics of different protein fractions in the endospem of developing maize kernel in normal, opaque-2 and QPM in response to the introgression of endosperm modifiers. Results revealed that albumin and globulin content decreases, whereas, prolamin, prolamin-like, glutelin-like, and glutelin content increases with kernel maturity. It has been observed that opaque-2 mutation affects protein expression at initial stages, whereas, the effect of endosperm modifiers was observed at the intermediate and later stages of kernel development. It has also been noted that prolamin, glutelin, and glutelin-like fractions can be used as quick markers for quality assessment for differentiating QPM varieties, even at the immature stage of kernel development. Overall, the present study implicates the role of different protein fractions in developing and utilizing nutritionally improved maize varieties.

Effect of spatial arrangement of push-pull companion plants on fall armyworm control and agronomic performance of two maize varieties in Ghana

2021 ◽  
pp. 105612
Author(s):  
Stephen Yeboah ◽  
Stella A. Ennin ◽  
Adama Ibrahim ◽  
Patricia Oteng-Darko ◽  
Daniel Mutyambai ◽  
...  
Keyword(s):  
Fall Armyworm ◽  
Spatial Arrangement ◽  
Agronomic Performance ◽  
Maize Varieties ◽  
Companion Plants

scholarly journals TTC3-Mediated Protein Quality Control, A Potential Mechanism for Cognitive Impairment

2021 ◽  
Author(s):  
Xu Zhou ◽  
Xiongjin Chen ◽  
Tingting Hong ◽  
Miaoping Zhang ◽  
Yujie Cai ◽  
...  
Keyword(s):  
Quality Control ◽  
Cognitive Impairment ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Ubiquitin Proteasome System ◽  
Research Progress ◽  
Repeat Domain ◽  
Ubiquitin Proteasome ◽  
Domain 3

AbstractThe tetrapeptide repeat domain 3 (TTC3) gene falls within Down's syndrome (DS) critical region. Cognitive impairment is a common phenotype of DS and Alzheimer’s disease (AD), and overexpression of TTC3 can accelerate cognitive decline, but the specific mechanism is unknown. The TTC3-mediated protein quality control (PQC) mechanism, similar to the PQC system, is divided into three parts: it acts as a cochaperone to assist proteins in folding correctly; it acts as an E3 ubiquitin ligase (E3s) involved in protein degradation processes through the ubiquitin–proteasome system (UPS); and it may also eventually cause autophagy by affecting mitochondrial function. Thus, this article reviews the research progress on the structure, function, and metabolism of TTC3, including the recent research progress on TTC3 in DS and AD; the role of TTC3 in cognitive impairment through PQC in combination with the abovementioned attributes of TTC3; and the potential targets of TTC3 in the treatment of such diseases.

Rye C-banding patterns and meiotic stability of hexaploid triticale (× Triticosecale) selections differing in kernel shriveling

Genome ◽  
1990 ◽  
Vol 33 (5) ◽  
pp. 686-689 ◽  
Author(s):  
Charles M. Papa ◽  
R. Morris ◽  
J. W. Schmidt
Keyword(s):  
Secale Cereale ◽  
Chromosome Banding ◽  
Agronomic Performance ◽  
Hexaploid Triticale ◽  
Kernel Development ◽  
Banding Patterns ◽  
C Banding ◽  
Meiotic Stability ◽  
Metaphase I

Two winter hexaploid triticale populations derived from the same cross were selected on the basis of grain appearance and agronomic performance. The five lines from 84LT402 showed more kernel shriveling than the four lines from 84LT401. The derived lines were analyzed for aneuploid frequencies, rye chromosome banding patterns, and meiotic stability to detect associations with kernel development. The aneuploid frequencies were 16% in 84LT401 and 18% in 84LT402. C-banding showed that both selection groups had all the rye chromosomes except 2R. The two groups had similar telomeric patterns but differed in the long-arm interstitial patterns of 4R and 5R. Compared with lines from 84LT402, those from 84LT401 had significantly fewer univalents and rod bivalents, and more paired arms at metaphase I; fewer laggards and bridges at anaphase I; and a higher frequency of normal tetrads. There were no significant differences among lines within each group for any meiotic character. Since there were no differences within or between groups in telomeric banding patterns, the differences in kernel shriveling and meiotic stability might be due to genotypic factors and (or) differences in the interstitial patterns of 4R and 5R. By selecting plump grains, lines with improved kernel characteristics along with improved meiotic stability are obtainable.Key words: triticale, meiotic stability, C-banding, Secale cereale, heterochromatin.

Abstract 88: A Crucial Role of BAG3 in Preventing Dilated Cardiomyopathy

2017 ◽  
Vol 121 (suppl_1) ◽  
Author(s):  
Xi Fang ◽  
Julius Bogomolovas ◽  
Wei Zhang ◽  
Tongbin Wu ◽  
Canzhao Liu ◽  
...  
Keyword(s):  
Heart Failure ◽  
Dilated Cardiomyopathy ◽  
Protein Quality ◽  
Contractile Function ◽  
Metabolic Stress ◽  
Insoluble Fraction ◽  
Therapeutic Benefit ◽  
Loss Of Function ◽  
Specific Subset

Defective protein quality control (PQC) systems are implicated in multiple diseases, with molecular chaperones/co-chaperones being critical to PQC. Cardiomyocytes are constantly challenged by mechanical and metabolic stress, placing great demand on the PQC system. Mutations and downregulation of the co-chaperone protein B cl-2- a ssociated athano g ene 3 (BAG3) are associated with cardiac myopathy and heart failure, and a BAG3 E455K mutation leads to Dilated cardiomyopathy (DCM). However, the role of BAG3 in the heart and mechanisms by which the E455K mutation lead to DCM remained obscure. Here, we found that cardiac-specific BAG3 knockout (CKO) and cardiac-specific E455K BAG3 knockin mice developed DCM. Comparable phenotypes in the two mutants demonstrated that the E455K mutation resulted in loss-of-function, and experiments revealed that the E455K mutation disrupted interaction between BAG3 and HSP70. In both mutants, decreased levels of small heat shock proteins (sHSPs) were observed, and a specific subset of proteins required for metabolic and contractile function of cardiomyocytes was enriched in the insoluble fraction. Together, these observations suggested that interaction between BAG3 and HSP70 was essential for BAG3 to stabilize sHSPs and maintain cardiomyocyte protein homeostasis. Our results provide new insight into the pathogenesis of heart failure caused by defects in BAG3 pathways, suggesting that increasing protein levels of BAG3 may be of therapeutic benefit in heart failure.

PINK1/Parkin in Neurodegenerative Disorders

2020 ◽  
pp. 282-301 ◽  
Author(s):  
Mukesh Pandey ◽  
Shakir Saleem ◽  
Himani Nautiyal ◽  
Faheem Hyder Pottoo ◽  
Md. Noushad Javed
Keyword(s):  
Quality Control ◽  
Neurodegenerative Disorders ◽  
Protein Quality ◽  
Surveillance Systems ◽  
Mutant Proteins ◽  
Subsequent Effect ◽  
Pink1 Gene ◽  
Disease Cell ◽  
Early Onset Parkinson’S Disease

PTEN-induced kinase 1 (PINK1), a mitochondrial serine/threonine-protein kinase encoded by the PINK1 gene, is thought to protect cells from stress-induced mitochondrial dysfunction. The activity of PINK1 facilitates the binding of Parkin protein with depolarized mitochondria to induce autophagy. Mutations of PINK1causes a type of autosomal recessive early-onset Parkinson's disease. Cell depends on the surveillance systems or mechanisms like protein quality control to handle the alterations in the proteins that are induced because of these mutations. These mutant proteins are found to be pathogenic and are reported to be related to various neurodegenerative disorders. This chapter focuses on the role of PINK1/Parkin in mitochondria quality control and its subsequent effect in neurodegeneration.

Protein Quality Control in Neurodegeneration and Neuroprotection

2020 ◽  
pp. 1-24
Author(s):  
Yasmeena Akhter ◽  
Jahangir Nabi ◽  
Hinna Hamid ◽  
Nahida Tabassum ◽  
Faheem Hyder Pottoo ◽  
...  
Keyword(s):  
Quality Control ◽  
Neurodegenerative Disorders ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Ubiquitin Proteasome System ◽  
Security System ◽  
Conformational Disorders ◽  
Ubiquitin Proteasome ◽  
Multi Level

Proteostasis is essential for regulating the integrity of the proteome. Disruption of proteostasis under some rigorous conditions leads to the aggregation and accumulation of misfolded toxic proteins, which plays a central role in the pathogenesis of protein conformational disorders. The protein quality control (PQC) system serves as a multi-level security system to shield cells from abnormal proteins. The intrinsic PQC systems maintaining proteostasis include the ubiquitin-proteasome system (UPS), chaperon-mediated autophagy (CMA), and autophagy-lysosome pathway (ALP) that serve to target misfolded proteins for unfolding, refolding, or degradation. Alterations of PQC systems in neurons have been implicated in the pathogenesis of various neurodegenerative disorders. This chapter provides an overview of PQC pathways to set a framework for discussion of the role of PQC in neurodegenerative disorders. Additionally, various pharmacological approaches targeting PQC are summarized.

scholarly journals Expanding Role of Ubiquitin in Translational Control

2020 ◽  
Vol 21 (3) ◽  
pp. 1151 ◽  
Author(s):  
Shannon E. Dougherty ◽  
Austin O. Maduka ◽  
Toshifumi Inada ◽  
Gustavo M. Silva
Keyword(s):  
Translational Control ◽  
Ribosomal Proteins ◽  
Ribosome Biogenesis ◽  
Rna Binding ◽  
Protein Quality ◽  
Rna Binding Proteins ◽  
Ubiquitin Chain ◽  
Molecular Aspects ◽  
And Function

The eukaryotic proteome has to be precisely regulated at multiple levels of gene expression, from transcription, translation, and degradation of RNA and protein to adjust to several cellular conditions. Particularly at the translational level, regulation is controlled by a variety of RNA binding proteins, translation and associated factors, numerous enzymes, and by post-translational modifications (PTM). Ubiquitination, a prominent PTM discovered as the signal for protein degradation, has newly emerged as a modulator of protein synthesis by controlling several processes in translation. Advances in proteomics and cryo-electron microscopy have identified ubiquitin modifications of several ribosomal proteins and provided numerous insights on how this modification affects ribosome structure and function. The variety of pathways and functions of translation controlled by ubiquitin are determined by the various enzymes involved in ubiquitin conjugation and removal, by the ubiquitin chain type used, by the target sites of ubiquitination, and by the physiologic signals triggering its accumulation. Current research is now elucidating multiple ubiquitin-mediated mechanisms of translational control, including ribosome biogenesis, ribosome degradation, ribosome-associated protein quality control (RQC), and redox control of translation by ubiquitin (RTU). This review discusses the central role of ubiquitin in modulating the dynamism of the cellular proteome and explores the molecular aspects responsible for the expanding puzzle of ubiquitin signals and functions in translation.

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