Regulation and Function of Protein S-Nitrosylation in Plant Stress

2013 ◽  
pp. 123-148 ◽  
Author(s):  
Gitto Thomas Kuruthukulangarakoola ◽  
Christian Lindermayr
Keyword(s):  
Plant Stress ◽  
Protein S ◽  
And Function

scholarly journals Structures and function of locked conformations of SARS-CoV-2 spike

2021 ◽  
Author(s):  
Kun Qu ◽  
Xiaoli Xiong ◽  
Katarzyna A. Ciazynska ◽  
Andrew P. Carter ◽  
John A. G. Briggs
Keyword(s):  
Receptor Binding ◽  
Functional Characterization ◽  
Protein S ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Neutral Ph ◽  
And Function ◽  
Cellular Compartments ◽  
Domain Dynamics ◽  
Spike Dynamics

AbstractThe spike protein (S) of SARS-CoV-2 has been observed in three distinct pre-fusion conformations: locked, closed and open. Of these, the locked conformation was not previously observed for SARS-CoV-1 S and its function remains poorly understood. Here we engineered a SARS-CoV-2 S protein construct “S-R/x3” to arrest SARS-CoV-2 spikes in the locked conformation by a disulfide bond. Using this construct we determined high-resolution structures revealing two distinct locked states, with or without the D614G substitution that has become fixed in the globally circulating SARS-CoV-2 strains. The D614G mutation induces a structural change in domain D from locked-1 to locked-2 conformation to alter spike dynamics, promoting transition into the closed conformation from which opening of the receptor binding domain is permitted. The transition from locked to closed conformations is additionally promoted by a change from low to neutral pH. We propose that the locked conformations of S are present in the acidic cellular compartments where virus is assembled and egresses. In this model, release of the virion into the neutral pH extracellular space would favour transition to the closed form which itself can stochastically transition into the open form. The S-R/x3 construct provides a tool for the further structural and functional characterization of the locked conformations of S, as well as how sequence changes might alter S assembly and regulation of receptor binding domain dynamics.

scholarly journals The Sequence, Structure and Function of the Plant Stress Protein LEA3

2021 ◽  
Vol 120 (3) ◽  
pp. 32a
Author(s):  
Karamjeet K. Singh ◽  
Steffen P. Graether
Keyword(s):  
Plant Stress ◽  
Stress Protein ◽  
Structure And Function ◽  
Sequence Structure ◽  
And Function

Computational identification of protein S-sulfenylation sites by incorporating the multiple sequence features information

2017 ◽  
Vol 13 (12) ◽  
pp. 2545-2550 ◽  
Author(s):  
Md. Mehedi Hasan ◽  
Dianjing Guo ◽  
Hiroyuki Kurata
Keyword(s):  
Protein Structure ◽  
Posttranslational Modification ◽  
Protein S ◽  
Structure And Function ◽  
Major Type ◽  
Multiple Sequence ◽  
Sequence Features ◽  
Cellular Processes ◽  
Computational Identification ◽  
And Function

Cysteine S-sulfenylation is a major type of posttranslational modification that contributes to protein structure and function regulation in many cellular processes.

Mechanism and function of DHHC S-acyltransferases

2013 ◽  
Vol 41 (1) ◽  
pp. 29-34 ◽  
Author(s):  
Maurine E. Linder ◽  
Benjamin C. Jennings
Keyword(s):  
Fatty Acids ◽  
Protein S ◽  
Enzyme Mechanism ◽  
Long Chain Fatty Acids ◽  
Post Translational Modification ◽  
Rich Domain ◽  
Cytoplasmic Face ◽  
Protein Membrane ◽  
And Function ◽  
Cysteine Rich Domain

Protein S-palmitoylation is a reversible post-translational modification of proteins with fatty acids. In the last 5 years, improved proteomic methods have increased the number of proteins identified as substrates for palmitoylation from tens to hundreds. Palmitoylation regulates protein membrane interactions, activity, trafficking and stability and can be constitutive or regulated by signalling inputs. A family of PATs (protein acyltransferases) is responsible for modifying proteins with palmitate or other long-chain fatty acids on the cytoplasmic face of cellular membranes. PATs share a signature DHHC (Asp-His-His-Cys) cysteine-rich domain that is the catalytic centre of the enzyme. The biomedical importance of members of this family is underscored by their association with intellectual disability, Huntington's disease and cancer in humans, and raises the possibility of DHHC PATs as targets for therapeutic intervention. In the present paper, we discuss recent progress in understanding enzyme mechanism, regulation and substrate specificity.

scholarly journals An atlas of Arabidopsis protein S-Acylation reveals its widespread role in plant cell organisation of and function

2020 ◽  
Author(s):  
Manoj Kumar ◽  
Paul Carr ◽  
Simon Turner
Keyword(s):  
Sequence Similarity ◽  
Protein S ◽  
Cysteine Residue ◽  
Cellulose Synthesis ◽  
Post Translational Modification ◽  
Cellular Functions ◽  
Ring Type ◽  
Arabidopsis Proteome ◽  
Arabidopsis Protein ◽  
And Function

AbstractS-acylation is the addition of a fatty acid to a cysteine residue of a protein. While this modification may profoundly alter protein behaviour, its effects on the function of plant proteins remains poorly characterised, largely as a result to the lack of basic information regarding which proteins are S-acylated and where in the proteins the modification occurs. In order to address this gap in our knowledge, we have performed a comprehensive analysis of plant protein S-acylation from 6 separate tissues. In our highest confidence group, we identified 5185 cysteines modified by S-acylation, which were located in 4891 unique peptides from 2643 different proteins. This represents around 9% of the entire Arabidopsis proteome and suggests an important role for S-acylation in many essential cellular functions including trafficking, signalling and metabolism. To illustrate the potential of this dataset, we focus on cellulose synthesis and confirm for the first time the S-acylation of all proteins known to be involved in cellulose synthesis and trafficking of the cellulose synthase complex. In the secondary cell walls, cellulose synthesis requires three different catalytic subunits (CESA4, CESA7 and CESA8) that all exhibit striking sequence similarity. While all three proteins have been widely predicted to possess a RING-type zinc finger at their N-terminus, for CESA4 and CESA8, we find evidence for S-acylation of cysteines in this region that is incompatible with any role in coordinating metal ions. We show that while CESA7 may possess a RING type domain, the same region of CESA4 and CESA8 appear to have evolved a very different structure. Together, the data suggests this study represents an atlas of S-acylation in Arabidopsis that will facilitate the broader study of this elusive post-translational modification in plants as well as demonstrates the importance of undertaking further work in this area.

scholarly journals The Structure, Activity, and Function of the SETD3 Protein Histidine Methyltransferase

Life ◽  
2021 ◽  
Vol 11 (10) ◽  
pp. 1040
Author(s):  
Apolonia Witecka ◽  
Sebastian Kwiatkowski ◽  
Takao Ishikawa ◽  
Jakub Drozak
Keyword(s):  
Protein S ◽  
Biological Processes ◽  
Set Domain ◽  
Hypoxic Conditions ◽  
Structure Activity ◽  
Mammalian Tissues ◽  
Bona Fide ◽  
And Function ◽  
Actin Protein ◽  
Cytoskeleton Integrity

SETD3 has been recently identified as a long sought, actin specific histidine methyltransferase that catalyzes the Nτ-methylation reaction of histidine 73 (H73) residue in human actin or its equivalent in other metazoans. Its homologs are widespread among multicellular eukaryotes and expressed in most mammalian tissues. SETD3 consists of a catalytic SET domain responsible for transferring the methyl group from S-adenosyl-L-methionine (AdoMet) to a protein substrate and a RuBisCO LSMT domain that recognizes and binds the methyl-accepting protein(s). The enzyme was initially identified as a methyltransferase that catalyzes the modification of histone H3 at K4 and K36 residues, but later studies revealed that the only bona fide substrate of SETD3 is H73, in the actin protein. The methylation of actin at H73 contributes to maintaining cytoskeleton integrity, which remains the only well characterized biological effect of SETD3. However, the discovery of numerous novel methyltransferase interactors suggests that SETD3 may regulate various biological processes, including cell cycle and apoptosis, carcinogenesis, response to hypoxic conditions, and enterovirus pathogenesis. This review summarizes the current advances in research on the SETD3 protein, its biological importance, and role in various diseases.

scholarly journals The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter semiSWEET

2020 ◽  
Author(s):  
Sunil Thomas
Keyword(s):  
In Silico ◽  
Transmembrane Domain ◽  
Sugar Transport ◽  
Protein S ◽  
M Protein ◽  
Sugar Transporter ◽  
Structural Protein ◽  
And Function ◽  
In Silico Analyses

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the disease COVID-19 that has decimated the health and economy of our planet. The virus causes the disease not only in people but also in companion and wild animals. People with diabetes are at risk of the disease. As yet we do not know why the virus is highly successful in causing the pandemic within 3 months of its first report. The structural proteins of SARS include, membrane glycoprotein (M), envelope protein (E), nucleocapsid protein (N) and the spike protein (S). The structure and function of the most abundant structural protein of SARS-CoV-2, the membrane (M) glycoprotein is not fully understood. Using in silico analyses we determined the structure and potential function of the M protein. In silico analyses showed that the M protein of SARS-CoV-2 has a triple helix bundle, form a single 3-transmembrane domain (TM), and are homologous to the prokaryotic sugar transport protein semiSWEET. The advantage and role of sugar transporter like structures in viruses are unknown. If they are involved in energy metabolism, they may aid in the rapid proliferation and replication of the virus. Biological experiments should be performed to validate the presence and function of the semiSWEET sugar transporter.

scholarly journals The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter semiSWEET

2020 ◽  
Author(s):  
Sunil Thomas
Keyword(s):  
In Silico ◽  
Transmembrane Domain ◽  
Sugar Transport ◽  
Protein S ◽  
M Protein ◽  
Sugar Transporter ◽  
Structural Protein ◽  
Sugar Transporters ◽  
And Function ◽  
In Silico Analyses

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the disease COVID-19 that has decimated the health and economy of our planet. The virus causes the disease not only in people but also in companion and wild animals. People with diabetes are at risk of the disease. As yet we do not know why the virus is highly successful in causing the pandemic within 3 months of its first report. The structural proteins of SARS include, membrane glycoprotein (M), envelope protein (E), nucleocapsid protein (N) and the spike protein (S). The structure and function of the most abundant structural protein of SARS-CoV-2, the membrane (M) glycoprotein is not fully understood. Using in silico analyses we determined the structure and potential function of the M protein. In silico analyses showed that the M protein of SARS-CoV-2 has a triple helix bundle, form a single 3-transmembrane domain (TM), and are homologous to the prokaryotic sugar transport protein semiSWEET. SemiSWEETs are related to the PQ-loop family that function as cargo receptors in vesicle transport, mediates movement of basic amino acids across lysosomal membranes, and is also involved in phospholipase flippase function. The advantage and role of sugar transporter-like structure in viruses is unknown. Endocytosis is critical for the internalization and maturation of RNA viruses, including SARS-CoV-2. Sucrose is involved in endosome and lysosome maturation and may also induce autophagy, pathways that help in the entry of the virus. It could be hypothesized that the semiSWEET sugar transporters could be used in multiple pathways that may aid in the rapid proliferation and replication of the virus. Biological experiments would validate the presence and function of the semiSWEET sugar transporter.

scholarly journals The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter semiSWEET

2020 ◽  
Author(s):  
Sunil Thomas
Keyword(s):  
In Silico ◽  
Transmembrane Domain ◽  
Sugar Transport ◽  
Protein S ◽  
M Protein ◽  
Sugar Transporter ◽  
Structural Protein ◽  
Sugar Transporters ◽  
And Function ◽  
In Silico Analyses

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the disease COVID-19 that has decimated the health and economy of our planet. The virus causes the disease not only in people but also in companion and wild animals. People with diabetes are at risk of the disease. As yet we do not know why the virus is highly successful in causing the pandemic within 3 months of its first report. The structural proteins of SARS include, membrane glycoprotein (M), envelope protein (E), nucleocapsid protein (N) and the spike protein (S). The structure and function of the most abundant structural protein of SARS-CoV-2, the membrane (M) glycoprotein is not fully understood. Using in silico analyses we determined the structure and potential function of the M protein. The M protein of SARS-CoV-2 is 98.6% similar to the M protein of bat SARS-CoV, maintains 98.2% homology with pangolin SARS-CoV, and has 90% homology with M protein of SARS-CoV; whereas, the similarity was only 38% with the M protein of MERS-CoV. In silico analyses showed that the M protein of SARS-CoV-2 has a triple helix bundle, form a single 3-transmembrane domain (TM), and are homologous to the prokaryotic sugar transport protein semiSWEET. SemiSWEETs are related to the PQ-loop family that function as cargo receptors in vesicle transport, mediates movement of basic amino acids across lysosomal membranes, and is also involved in phospholipase flippase function. The advantage and role of sugar transporter-like structure in viruses is unknown. Endocytosis is critical for the internalization and maturation of RNA viruses, including SARS-CoV-2. Sucrose is involved in endosome and lysosome maturation and may also induce autophagy, pathways that help in the entry of the virus. It could be hypothesized that the semiSWEET sugar transporters could be used in multiple pathways that may aid in the rapid proliferation and replication of the virus. Biological experiments would validate the presence and function of the semiSWEET sugar transporter.

scholarly journals The Physiology of Protein S-acylation

2015 ◽  
Vol 95 (2) ◽  
pp. 341-376 ◽  
Author(s):  
Luke H. Chamberlain ◽  
Michael J. Shipston
Keyword(s):  
Physiological Function ◽  
Protein S ◽  
Membrane Receptors ◽  
Structural Proteins ◽  
Proteomic Profiling ◽  
Physiological Processes ◽  
Challenges And Opportunities ◽  
And Function ◽  
Structure Assembly ◽  
Control Protein

Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is emerging as a ubiquitous mechanism to control the properties and function of a diverse array of proteins and consequently physiological processes. S-acylation results from the enzymatic addition of long-chain lipids, most typically palmitate, onto intracellular cysteine residues of soluble and transmembrane proteins via a labile thioester linkage. Addition of lipid results in increases in protein hydrophobicity that can impact on protein structure, assembly, maturation, trafficking, and function. The recent explosion in global S-acylation (palmitoyl) proteomic profiling as a result of improved biochemical tools to assay S-acylation, in conjunction with the recent identification of enzymes that control protein S-acylation and de-acylation, has opened a new vista into the physiological function of S-acylation. This review introduces key features of S-acylation and tools to interrogate this process, and highlights the eclectic array of proteins regulated including membrane receptors, ion channels and transporters, enzymes and kinases, signaling adapters and chaperones, cell adhesion, and structural proteins. We highlight recent findings correlating disruption of S-acylation to pathophysiology and disease and discuss some of the major challenges and opportunities in this rapidly expanding field.

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