scholarly journals On the move: Redox –dependent protein relocation

2019 ◽  
Author(s):  
Christine H. Foyer ◽  
Alison Baker ◽  
Megan Wright ◽  
Imogen A. Sparkes ◽  
Amna Mhamdi ◽  
...  
Keyword(s):  
Growth And Development ◽  
De Novo ◽  
Eukaryotic Cells ◽  
Cellular Compartment ◽  
Post Translational Modifications ◽  
Multiple Functions ◽  
Membrane Compartments ◽  
Dependent Protein ◽  
Protein Complement

ABSTRACTCompartmentation of proteins and processes is a defining feature of eukaryotic cells. The growth and development of organisms is critically dependent on the accurate sorting of proteins within cells. The mechanisms by which cytosol-synthesized proteins are delivered to the membranes and membrane compartments have been extensively characterised. However, the protein complement of any given compartment is not precisely fixed and some proteins can move between compartments in response to metabolic or environmental triggers. The mechanisms and processes that mediate such relocation events are largely uncharacterized. Many proteins can in addition perform multiple functions, catalyzing alternative reactions or performing structural, non-enzymatic functions. These alternative functions can be equally important functions in each cellular compartment. Such proteins are generally not dual targeted proteins in the classic sense of having targeting sequences that directde novosynthesised proteins to specific cellular locations. Accumulating evidence suggests that redox post-translational modifications (PTMs) can control the compartmentation of many such proteins, including antioxidant and/or redox associated enzymes.

Post-translational modifications of the regulatory subunits of cAMP-dependent protein kinases during G1/S progression

2001 ◽  
Vol 324 (1) ◽  
pp. 23-31
Author(s):  
Marina Yassenko ◽  
Patrice Thérond ◽  
Danièle Évain-Brion ◽  
Guy Keryer
Keyword(s):  
Protein Kinases ◽  
Post Translational Modifications ◽  
Regulatory Subunits ◽  
Dependent Protein

Metabolism-driven post-translational modifications of H3K9 in early bovine embryos

Reproduction ◽  
2021 ◽  
Vol 162 (3) ◽  
pp. 181-191
Author(s):  
Jessica Ispada ◽  
Aldcejam Martins da Fonseca Junior ◽  
Otávio Luiz Ramos Santos ◽  
Camila Bruna de Lima ◽  
Erika Cristina dos Santos ◽  
...  
Keyword(s):  
Metabolic Pathways ◽  
Developmental Stages ◽  
De Novo ◽  
Blastocyst Stage ◽  
Developmental Model ◽  
Bovine Embryos ◽  
Acetyl Coa ◽  
Post Translational Modifications ◽  
The Relationship ◽  
Different Levels

Metabolic and molecular profiles were reported as different for bovine embryos with distinct kinetics during the first cleavages. In this study, we used this same developmental model (fast vs slow) to determine if the relationship between metabolism and developmental kinetics affects the levels of acetylation or tri-methylation at histone H3 lysine 9 (H3K9ac and H3K9me3, respectively). Fast and slow developing embryos presented different levels of H3K9ac and H3K9me3 from the earliest stages of development (40 and 96 hpi) and up to the blastocyst stage. For H3K9me3, both groups of embryos presented a wave of demethylation and de novo methylation, although it was more pronounced in fast than slow embryos, resulting in blastocysts with higher levels of this mark. The H3K9ac reprogramming profile was distinct between kinetics groups. While slow embryos presented a wave of deacetylation, followed by an increase in this mark at the blastocyst stage, fast embryos reduced this mark throughout all the developmental stages studied. H3K9me3 differences corresponded to writer and eraser transcript levels, while H3K9ac patterns were explained by metabolism-related gene expression. To verify if metabolic differences could alter levels of H3K9ac, embryos were cultured with sodium-iodoacetate (IA) or dichloroacetate (DCA) to disrupt the glycolytic pathway or increase acetyl-CoA production, respectively. IA reduced H3K9ac while DCA increased H3K9ac in blastocysts. Concluding, H3K9me3 and H3K9ac patterns differ between embryos with different kinetics, the second one explained by metabolic pathways involved in acetyl-CoA production. So far, this is the first study demonstrating a relationship between metabolic differences and histone post-translational modifications in bovine embryos.

scholarly journals Heterologous expression and purification of recombinant human protoporphyrinogen oxidase IX: A comparative study

PLoS ONE ◽  
2021 ◽  
Vol 16 (11) ◽  
pp. e0259837
Author(s):  
Zora Novakova ◽  
Daria Khuntsaria ◽  
Marketa Gresova ◽  
Jana Mikesova ◽  
Barbora Havlinova ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Mammalian Cells ◽  
Specific Activity ◽  
Eukaryotic Cells ◽  
Post Translational Modifications ◽  
Protoporphyrinogen Oxidase ◽  
Intracellular Targeting ◽  
Alternative Systems ◽  
Protein Functions ◽  
The Impact

Human protoporphyrinogen oxidase IX (hPPO) is an oxygen-dependent enzyme catalyzing the penultimate step in the heme biosynthesis pathway. Mutations in the enzyme are linked to variegate porphyria, an autosomal dominant metabolic disease. Here we investigated eukaryotic cells as alternative systems for heterologous expression of hPPO, as the use of a traditional bacterial-based system failed to produce several clinically relevant hPPO variants. Using bacterially-produced hPPO, we first analyzed the impact of N-terminal tags and various detergent on hPPO yield, and specific activity. Next, the established protocol was used to compare hPPO constructs heterologously expressed in mammalian HEK293T17 and insect Hi5 cells with prokaryotic overexpression. By attaching various fusion partners at the N- and C-termini of hPPO we also evaluated the influence of the size and positioning of fusion partners on expression levels, specific activity, and intracellular targeting of hPPO fusions in mammalian cells. Overall, our results suggest that while enzymatically active hPPO can be heterologously produced in eukaryotic systems, the limited availability of the intracellular FAD co-factor likely negatively influences yields of a correctly folded protein making thus the E.coli a system of choice for recombinant hPPO overproduction. At the same time, PPO overexpression in eukaryotic cells might be preferrable in cases when the effects of post-translational modifications (absent in bacteria) on target protein functions are studied.

Lipoxygenases in Plants -Their Role in Development and Stress Response

1996 ◽  
Vol 51 (3-4) ◽  
pp. 123-138 ◽  
Author(s):  
Sabine Rosahl
Keyword(s):  
Fatty Acids ◽  
Growth And Development ◽  
Physiological Function ◽  
Signal Molecules ◽  
Antimicrobial Compounds ◽  
Multiple Functions ◽  
Acid Metabolites ◽  
Wound Stress ◽  
Fatty Acid Metabolites ◽  
Lox Products

Abstract Lipoxygenases catalyze the hydroperoxidation of polyunsaturated fatty acids and thus the first step in the synthesis of fatty acid metabolites in plants. Products of the LOX pathway have multiple functions as growth regulators, antimicrobial compounds, flavours and odours as well as signal molecules. Based on the effects of LOX products or on the correlation of increases in LOX protein and the onset of specific processes, a physiological function for LOXs has been proposed for growth and development and for the plant response to patho­gen infection and wound stress.

scholarly journals Altered miRNA and mRNA Expression in Sika Deer Skeletal Muscle with Age

Genes ◽  
2020 ◽  
Vol 11 (2) ◽  
pp. 172
Author(s):  
Boyin Jia ◽  
Yuan Liu ◽  
Qining Li ◽  
Jiali Zhang ◽  
Chenxia Ge ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Growth And Development ◽  
Molecular Mechanisms ◽  
Muscle Development ◽  
Sika Deer ◽  
De Novo ◽  
Expression Profiles ◽  
Differentially Expressed ◽  
Growth Development ◽  
Development And Aging

Studies of the gene and miRNA expression profiles associated with the postnatal late growth, development, and aging of skeletal muscle are lacking in sika deer. To understand the molecular mechanisms of the growth and development of sika deer skeletal muscle, we used de novo RNA sequencing (RNA-seq) and microRNA sequencing (miRNA-seq) analyses to determine the differentially expressed (DE) unigenes and miRNAs from skeletal muscle tissues at 1, 3, 5, and 10 years in sika deer. A total of 51,716 unigenes, 171 known miRNAs, and 60 novel miRNAs were identified based on four mRNA and small RNA libraries. A total of 2,044 unigenes and 11 miRNAs were differentially expressed between adolescence and juvenile sika deer, 1,946 unigenes and 4 miRNAs were differentially expressed between adult and adolescent sika deer, and 2,209 unigenes and 1 miRNAs were differentially expressed between aged and adult sika deer. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analyses showed that DE unigenes and miRNA were mainly related to energy and substance metabolism, processes that are closely associate with the growth, development, and aging of skeletal muscle. We also constructed mRNA–mRNA and miRNA–mRNA interaction networks related to the growth, development, and aging of skeletal muscle. The results show that mRNA (Myh1, Myh2, Myh7, ACTN3, etc.) and miRNAs (miR-133a, miR-133c, miR-192, miR-151-3p, etc.) may play important roles in muscle growth and development, and mRNA (WWP1, DEK, UCP3, FUS, etc.) and miRNAs (miR-17-5p, miR-378b, miR-199a-5p, miR-7, etc.) may have key roles in muscle aging. In this study, we determined the dynamic miRNA and unigenes transcriptome in muscle tissue for the first time in sika deer. The age-dependent miRNAs and unigenes identified will offer insights into the molecular mechanism underlying muscle development, growth, and maintenance and will also provide valuable information for sika deer genetic breeding.

scholarly journals De novo genome assembly of Candida glabrata reveals cell wall protein complement and structure of dispersed tandem repeat arrays

2020 ◽  
Vol 113 (6) ◽  
pp. 1209-1224
Author(s):  
Zhuwei Xu ◽  
Brian Green ◽  
Nicole Benoit ◽  
Michael Schatz ◽  
Sarah Wheelan ◽  
...  
Keyword(s):  
Cell Wall ◽  
Tandem Repeat ◽  
Genome Assembly ◽  
Candida Glabrata ◽  
De Novo ◽  
Cell Wall Protein ◽  
De Novo Genome Assembly ◽  
Protein Complement

scholarly journals The Spectrinome: The Interactome of a Scaffold Protein Creating Nuclear and Cytoplasmic Connectivity and Function

2019 ◽  
Vol 244 (15) ◽  
pp. 1273-1302 ◽  
Author(s):  
Steven R. Goodman ◽  
Daniel Johnson ◽  
Steven L. Youngentob ◽  
David Kakhniashvili
Keyword(s):  
Cell Surface ◽  
Intracellular Signaling ◽  
Cellular Protein ◽  
Human Diseases ◽  
Scaffolding Protein ◽  
Eukaryotic Cells ◽  
Cellular Functions ◽  
Cellular Compartment ◽  
Atlas Data ◽  
And Function

We provide a review of Spectrin isoform function in the cytoplasm, the nucleus, the cell surface, and in intracellular signaling. We then discuss the importance of Spectrin’s E2/E3 chimeric ubiquitin conjugating and ligating activity in maintaining cellular homeostasis. Finally we present spectrin isoform subunit specific human diseases. We have created the Spectrinome, from the Human Proteome, Human Reactome and Human Atlas data and demonstrated how it can be a useful tool in visualizing and understanding spectrins myriad of cellular functions. Impact statement Spectrin was for the first 12 years after its discovery thought to be found only in erythrocytes. In 1981, Goodman and colleagues 1 found that spectrin-like molecules were ubiquitously found in non-erythroid cells leading to a great multitude of publications over the next thirty eight years. The discovery of multiple spectrin isoforms found associated with every cellular compartment, and representing 2-3% of cellular protein, has brought us to today’s understanding that spectrin is a scaffolding protein, with its own E2/E3 chimeric ubiquitin conjugating ligating activity that is involved in virtually every cellular function. We cover the history, localized functions of spectrin isoforms, human diseases caused by mutations, and provide the spectrinome: a useful tool for understanding the myriad of functions for one of the most important proteins in all eukaryotic cells.

1,25-Dihydroxyvitamin D3 Affects the Synthesis, Phosphorylation and in vitro Calmodulin Binding of Myoblast Cytoskeletal Proteins

1990 ◽  
Vol 45 (11-12) ◽  
pp. 1156-1160 ◽  
Author(s):  
Alicia Brunner ◽  
Ana R. de Boland
Keyword(s):  
Actinomycin D ◽  
De Novo ◽  
Cytoskeletal Proteins ◽  
Dihydroxyvitamin D3 ◽  
Calmodulin Binding ◽  
Isoelectric Points ◽  
Dependent Protein ◽  
Molecular Masses ◽  
Binding Component

Abstract Incubation of chick embryo myoblasts with 1,25-dihydroxyvitam in D3 [1,25(OH)2D3] (10-10 M , 24 h). markedly stimulated the incorporation of [3H]leucine into total cytoskeletal proteins and this effect was abolished when the sterol treatment was performed in the presence of cycloheximide or actinomycin D. 1,2 5 (OH)2D3 selectively stimulated the de novo synthesis of several proteins with apparent molecular masses (isoelectric points) of 220 kDa (6.1 and 9.7), 150 kDa (7.5), 110 kDa (7.2), 68 kDa (9.5, 7.5 and 4.5), 50 kDa (8.5), 44 kDa (6.3), 27 kDa (7.8) and 15 kDa (5.5). Labelling of proteins with [125I]calmodulin after their separation on SDS-polyacrylamide gels showed that 1,25(O H)2D3-dependent protein of 110 kDa is the major calmodulin-binding component of myoblasts cytoskeleton. In addition , the sterol increased the phosphorylation of several cytoskeletal proteins including that of 110 and 15 kDa whose synthesis potentiates.

scholarly journals Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae

2017 ◽  
Vol 37 (11) ◽  
Author(s):  
Jayasankar Mohanakrishnan Kaimal ◽  
Ganapathi Kandasamy ◽  
Fabian Gasser ◽  
Claes Andréasson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Protein Aggregation ◽  
Yeast Cells ◽  
Eukaryotic Cells ◽  
Content Type ◽  
Dependent Protein ◽  
And Function ◽  
Cellular Dysfunction

ABSTRACT Protein aggregation is intimately associated with cellular stress and is accelerated during aging, disease, and cellular dysfunction. Yeast cells rely on the ATP-consuming chaperone Hsp104 to disaggregate proteins together with Hsp70. Hsp110s are ancient and abundant chaperones that form complexes with Hsp70. Here we provide in vivo data showing that the Saccharomyces cerevisiae Hsp110s Sse1 and Sse2 are essential for Hsp104-dependent protein disaggregation. Following heat shock, complexes of Hsp110 and Hsp70 are recruited to protein aggregates and function together with Hsp104 in the disaggregation process. In the absence of Hsp110, targeting of Hsp70 and Hsp104 to the aggregates is impaired, and the residual Hsp104 that still reaches the aggregates fails to disaggregate. Thus, coordinated activities of both Hsp104 and Hsp110 are required to reactivate aggregated proteins. These findings have important implications for the understanding of how eukaryotic cells manage misfolded and amyloid proteins.

scholarly journals Functional Analysis of the Protein Machinery Required for Transport of Lipopolysaccharide to the Outer Membrane of Escherichia coli

2008 ◽  
Vol 190 (13) ◽  
pp. 4460-4469 ◽  
Author(s):  
Paola Sperandeo ◽  
Fion K. Lau ◽  
Andrea Carpentieri ◽  
Cristina De Castro ◽  
Antonio Molinaro ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Biosynthetic Pathway ◽  
De Novo ◽  
Gram Negative Bacteria ◽  
Membrane Structures ◽  
Cellular Compartment ◽  
Gram Negative ◽  
Outer Leaflet ◽  
Assembly Pathway

ABSTRACT Lipopolysaccharide (LPS) is an essential component of the outer membrane (OM) in most gram-negative bacteria, and its structure and biosynthetic pathway are well known. Nevertheless, the mechanisms of transport and assembly of this molecule at the cell surface are poorly understood. The inner membrane (IM) transport protein MsbA is responsible for flipping LPS across the IM. Additional components of the LPS transport machinery downstream of MsbA have been identified, including the OM protein complex LptD/LptE (formerly Imp/RlpB), the periplasmic LptA protein, the IM-associated cytoplasmic ATP binding cassette protein LptB, and LptC (formerly YrbK), an essential IM component of the LPS transport machinery characterized in this work. Here we show that depletion of any of the proteins mentioned above leads to common phenotypes, including (i) the presence of abnormal membrane structures in the periplasm, (ii) accumulation of de novo-synthesized LPS in two membrane fractions with lower density than the OM, and (iii) accumulation of a modified LPS, which is ligated to repeating units of colanic acid in the outer leaflet of the IM. Our results suggest that LptA, LptB, LptC, LptD, and LptE operate in the LPS assembly pathway and, together with other as-yet-unidentified components, could be part of a complex devoted to the transport of LPS from the periplasmic surface of the IM to the OM. Moreover, the location of at least one of these five proteins in every cellular compartment suggests a model for how the LPS assembly pathway is organized and ordered in space.

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