scholarly journals ConCysFind: a pipeline tool to predict conserved amino acids of protein sequences across the plant kingdom

2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Marten Moore ◽  
Corinna Wesemann ◽  
Nikolaj Gossmann ◽  
Arne Sahm ◽  
Jan Krüger ◽  
...  
Keyword(s):  
Phylogenetic Trees ◽  
Translation Elongation ◽  
Web Based ◽  
Post Translational Modifications ◽  
Plant Kingdom ◽  
Multiple Alignments ◽  
Biochemical Assays ◽  
Evolutionarily Conserved ◽  
Redox Sensitivity ◽  
Conserved Amino Acids

Abstract Background Post-translational modifications (PTM) of amino acid (AA) side chains in peptides control protein structure and functionality. PTMs depend on the specific AA characteristics. The reactivity of cysteine thiol-based PTMs are unique among all proteinaceous AA. This pipeline aims to ease the identification of conserved AA of polypeptides or protein families based on the phylogenetic occurrence in the plant kingdom. The tool is customizable to include any species. The degree of AA conservation is taken as indicator for structural and functional significance, especially for PTM-based regulation. Further, this pipeline tool gives insight into the evolution of these potentially regulatory important peptides. Results The web-based or stand-alone pipeline tool Conserved Cysteine Finder (ConCysFind) was developed to identify conserved AA such as cysteine, tryptophan, serine, threonine, tyrosin and methionine. ConCysFind evaluates multiple alignments considering the proteome of 21 plant species. This exemplar study focused on Cys as evolutionarily conserved target for multiple redox PTM. Phylogenetic trees and tables with the compressed results of the scoring algorithm are generated for each Cys in the query polypeptide. Analysis of 33 translation elongation and release factors alongside of known redox proteins from Arabidopsis thaliana for conserved Cys residues confirmed the suitability of the tool for identifying conserved and functional PTM sites. Exemplarily, the redox sensitivity of cysteines in the eukaryotic release factor 1-1 (eRF1-1) was experimentally validated. Conclusion ConCysFind is a valuable tool for prediction of new potential protein PTM targets in a broad spectrum of species, based on conserved AA throughout the plant kingdom. The identified targets were successfully verified through protein biochemical assays. The pipeline is universally applicable to other phylogenetic branches by customization of the database.

scholarly journals Visual Comparison of Phylogenetic Trees Through iPhyloC, a New Interactive Web-based Framework

2021 ◽  
Author(s):  
Muhsen Hammoud ◽  
Charles Morphy Santos ◽  
Joao Paulo Gois
Keyword(s):  
Phylogenetic Trees ◽  
Binary Trees ◽  
Automatic Identification ◽  
Structural Comparison ◽  
Web Based ◽  
Visual Comparison ◽  
Large Trees ◽  
Cross Platform ◽  
The Common ◽  
Intuitive Design

Current side-by-side phylogenetic trees comparison frameworks face two issues: (1) accepting binary trees as input, and (2) assuming input trees having identical or highly overlapping taxa. We present a task abstraction of the problem of side-by-side comparison of two phylogenetic trees and propose a set-based measure for detailed structural comparison between two phylogenetic trees, which can be non-binary and not highly overlapping. iPhyloC is an interactive web-based framework including automatic identification of the common taxa in both trees, comparing input trees in several modes, intuitive design, high usability, scalability to large trees, and cross-platform support. iPhyloC was tested in hypothetical and real biological examples.

scholarly journals iProteinDB: an integrative database of Drosophila post-translational modifications

2018 ◽  
Author(s):  
Yanhui Hu ◽  
Richelle Sopko ◽  
Verena Chung ◽  
Romain A. Studer ◽  
Sean D. Landry ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Protein Function ◽  
Large Scale ◽  
Model Organisms ◽  
General Strategy ◽  
Post Translational Modification ◽  
Post Translational Modifications ◽  
Functional Sites ◽  
Evolutionarily Conserved ◽  
And Function

AbstractPost-translational modification (PTM) serves as a regulatory mechanism for protein function, influencing stability, protein interactions, activity and localization, and is critical in many signaling pathways. The best characterized PTM is phosphorylation, whereby a phosphate is added to an acceptor residue, commonly serine, threonine and tyrosine. As proteins are often phosphorylated at multiple sites, identifying those sites that are important for function is a challenging problem. Considering that many phosphorylation sites may be non-functional, prioritizing evolutionarily conserved phosphosites provides a general strategy to identify the putative functional sites with regards to regulation and function. To facilitate the identification of conserved phosphosites, we generated a large-scale phosphoproteomics dataset from Drosophila embryos collected from six closely-related species. We built iProteinDB (https://www.flyrnai.org/tools/iproteindb/), a resource integrating these data with other high-throughput PTM datasets, including vertebrates, and manually curated information for Drosophila. At iProteinDB, scientists can view the PTM landscape for any Drosophila protein and identify predicted functional phosphosites based on a comparative analysis of data from closely-related Drosophila species. Further, iProteinDB enables comparison of PTM data from Drosophila to that of orthologous proteins from other model organisms, including human, mouse, rat, Xenopus laevis, Danio rerio, and Caenorhabditis elegans.

scholarly journals Sensing and signaling of oxidative stress in chloroplasts by inactivation of the SAL1 phosphoadenosine phosphatase

2016 ◽  
Vol 113 (31) ◽  
pp. E4567-E4576 ◽  
Author(s):  
Kai Xun Chan ◽  
Peter D. Mabbitt ◽  
Su Yin Phua ◽  
Jonathan W. Mueller ◽  
Nazia Nisar ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Intracellular Signaling ◽  
Redox Regulation ◽  
Sulfur Metabolism ◽  
Plant Kingdom ◽  
Disulfide Formation ◽  
Redox Poise ◽  
Redox Sensitivity ◽  
Stress Sensing ◽  
Retrograde Signal

Intracellular signaling during oxidative stress is complex, with organelle-to-nucleus retrograde communication pathways ill-defined or incomplete. Here we identify the 3′-phosphoadenosine 5′-phosphate (PAP) phosphatase SAL1 as a previously unidentified and conserved oxidative stress sensor in plant chloroplasts. Arabidopsis thaliana SAL1 (AtSAL1) senses changes in photosynthetic redox poise, hydrogen peroxide, and superoxide concentrations in chloroplasts via redox regulatory mechanisms. AtSAL1 phosphatase activity is suppressed by dimerization, intramolecular disulfide formation, and glutathionylation, allowing accumulation of its substrate, PAP, a chloroplast stress retrograde signal that regulates expression of plastid redox associated nuclear genes (PRANGs). This redox regulation of SAL1 for activation of chloroplast signaling is conserved in the plant kingdom, and the plant protein has evolved enhanced redox sensitivity compared with its yeast ortholog. Our results indicate that in addition to sulfur metabolism, SAL1 orthologs have evolved secondary functions in oxidative stress sensing in the plant kingdom.

scholarly journals Role of post-translational modifications at the β-subunit ectodomain in complex association with a promiscuous plant P4-ATPase

2016 ◽  
Vol 473 (11) ◽  
pp. 1605-1615 ◽  
Author(s):  
Sara R. Costa ◽  
Magdalena Marek ◽  
Kristian B. Axelsen ◽  
Lisa Theorin ◽  
Thomas G. Pomorski ◽  
...  
Keyword(s):  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Β Subunit ◽  
Post Translational Modifications ◽  
Functional Roles ◽  
Evolutionarily Conserved ◽  
A Site ◽  
P Type ◽  
Cell Division Control

P-type ATPases of subfamily IV (P4-ATPases) constitute a major group of phospholipid flippases that form heteromeric complexes with members of the Cdc50 (cell division control 50) protein family. Some P4-ATPases interact specifically with only one β-subunit isoform, whereas others are promiscuous and can interact with several isoforms. In the present study, we used a site-directed mutagenesis approach to assess the role of post-translational modifications at the plant ALIS5 β-subunit ectodomain in the functionality of the promiscuous plant P4-ATPase ALA2. We identified two N-glycosylated residues, Asn181 and Asn231. Whereas mutation of Asn231 seems to have a small effect on P4-ATPase complex formation, mutation of evolutionarily conserved Asn181 disrupts interaction between the two subunits. Of the four cysteine residues located in the ALIS5 ectodomain, mutation of Cys86 and Cys107 compromises complex association, but the mutant β-subunits still promote complex trafficking and activity to some extent. In contrast, disruption of a conserved disulfide bond between Cys158 and Cys172 has no effect on the P4-ATPase complex. Our results demonstrate that post-translational modifications in the β-subunit have different functional roles in different organisms, which may be related to the promiscuity of the P4-ATPase.

scholarly journals ClonArch: Visualizing the Spatial Clonal Architecture of Tumors

2020 ◽  
Author(s):  
Jiaqi Wu ◽  
Mohammed El-Kebir
Keyword(s):  
Visual Analytics ◽  
Phylogenetic Trees ◽  
Cancer Genomics ◽  
Clonal Evolution ◽  
Response To Treatment ◽  
Intratumor Heterogeneity ◽  
Tumor Evolution ◽  
Web Based ◽  
Clonal Architecture ◽  
Spatial Coordinates

AbstractMotivationCancer is caused by the accumulation of somatic mutations that lead to the formation of distinct populations of cells, called clones. The resulting clonal architecture is the main cause of relapse and resistance to treatment. With decreasing costs in DNA sequencing technology, rich cancer genomics datasets with many spatial sequencing samples are becoming increasingly available, enabling the inference of high-resolution tumor clones and prevalences across different spatial coordinates. While temporal and phylogenetic aspects of tumor evolution, such as clonal evolution over time and clonal response to treatment, are commonly visualized in various clonal evolution diagrams, visual analytics methods that reveal the spatial clonal architecture are missing.ResultsThis paper introduces ClonArch, a web-based tool to interactively visualize the phylogenetic tree and spatial distribution of clones in a single tumor mass. ClonArch uses the marching squares algorithm to draw closed boundaries representing the presence of clones in a real or simulated tumor. ClonArch enables researchers to examine the spatial clonal architecture of a subset of relevant mutations at different prevalence thresholds and across multiple phylogenetic trees. In addition to simulated tumors with varying number of biopsies, we demonstrate the use of ClonArch on a hepatocellular carcinoma tumor with ~280 sequencing biopsies. ClonArch provides an automated way to interactively examine the spatial clonal architecture of a tumor, facilitating clinical and biological interpretations of the spatial aspects of intratumor heterogeneity.Availabilityhttps://github.com/elkebir-group/ClonArch

scholarly journals Pharmosome: an integrative and collective database for exploration and analysis of single nucleotide polymorphisms associated with disease

F1000Research ◽  
2020 ◽  
Vol 9 ◽  
pp. 14 ◽  
Author(s):  
Peter T. Habib ◽  
Alsamman M. Alsamman ◽  
Sameh E. Hassanein ◽  
Kerolos M. Yousef ◽  
Aladdin Hamwieh
Keyword(s):  
Phylogenetic Trees ◽  
Drug Response ◽  
Nucleotide Polymorphisms ◽  
Nucleotide Polymorphism ◽  
Single Nucleotide ◽  
Web Based ◽  
Consensus Sequences ◽  
Python Programming ◽  
User Friendly ◽  
To Receive

Current single nucleotide polymorphism (SNP) databases are limited to a narrow set of SNPs, which has led to a lack of interactivity between different databases, limited tools to analyze and manipulate the already existing data, and complexity in the graphical user interface. Here we introduce Pharmosome, a web-based, user-friendly and collective database for more than 30,000 human disease-related SNPs, with dynamic pipelines to explore SNPs associated with disease development, drug response and the pathways shared between different genes related to these SNPs. Pharmosome implements several tools to design primers to detect SNPs in large genomes and facilitates analysis of different SNPs to determine relationships between them by aligning sequences, constructing phylogenetic trees, and providing consensus sequences illustrating the connections between SNPs. Pharmosome was written in the Python programming language using the Django web framework in combination with HTML, CSS, and JavaScript to receive user inputs, and process and export the sorted result to the interface. Pharmosome is available from: https://pharmosome.herokuapp.com/.

scholarly journals SwissPalm: Protein Palmitoylation database

F1000Research ◽  
2015 ◽  
Vol 4 ◽  
pp. 261 ◽  
Author(s):  
Mathieu Blanc ◽  
Fabrice David ◽  
Laurence Abrami ◽  
Daniel Migliozzi ◽  
Florence Armand ◽  
...  
Keyword(s):  
Protein S ◽  
Biological Processes ◽  
Post Translational Modification ◽  
Chemical Methods ◽  
Post Translational Modifications ◽  
P Protein ◽  
Multiple Alignments ◽  
Protein Palmitoylation ◽  
Recent Developments ◽  
Pathway Analyses

Protein S-palmitoylation is a reversible post-translational modification that regulates many key biological processes, although the full extent and functions of protein S-palmitoylation remain largely unexplored. Recent developments of new chemical methods have allowed the establishment of palmitoyl-proteomes of a variety of cell lines and tissues from different species.  As the amount of information generated by these high-throughput studies is increasing, the field requires centralization and comparison of this information. Here we present SwissPalm (http://swisspalm.epfl.ch), our open, comprehensive, manually curated resource to study protein S-palmitoylation. It currently encompasses more than 5000 S-palmitoylated protein hits from seven species, and contains more than 500 specific sites of S-palmitoylation. SwissPalm also provides curated information and filters that increase the confidence in true positive hits, and integrates predictions of S-palmitoylated cysteine scores, orthologs and isoform multiple alignments. Systems analysis of the palmitoyl-proteome screens indicate that 10% or more of the human proteome is susceptible to S-palmitoylation. Moreover, ontology and pathway analyses of the human palmitoyl-proteome reveal that key biological functions involve this reversible lipid modification. Comparative analysis finally shows a strong crosstalk between S-palmitoylation and other post-translational modifications. Through the compilation of data and continuous updates, SwissPalm will provide a powerful tool to unravel the global importance of protein S-palmitoylation.

Hanseniaspora terricola sp. nov., an ascomycetous yeast isolated from Tibet

2019 ◽  
Vol 71 (3) ◽  
Author(s):  
Ze Liu ◽  
Man-Man Wang ◽  
Gui-Shuang Wang ◽  
Ai-Hua Li ◽  
Wangmu ◽  
...  
Keyword(s):  
Phylogenetic Trees ◽  
Novel Species ◽  
Elongation Factor ◽  
Its Region ◽  
Original Description ◽  
Ascomycetous Yeast ◽  
Translation Elongation ◽  
Separate Branch ◽  
Pr China ◽  
Elongation Factor 1

Eight apiculate strains isolated from Tibet, PR China, were identified as Hanseniaspora taiwanica and a novel species of Hanseniaspora based on the sequence analysis of the ITS region, the D1/D2 domains of the LSU rRNA and the translation elongation factor 1-a (TEF1) gene. Among them, four strains with identical sequences of D1/D2 and ITS formed a separate branch from the known Hanseniaspora species in the phylogenetic trees, and differed from the known species by at least 17 (3 %) nucleotide (nt) substitutions in the D1/D2 domains and more than 6 % substitutions and inserts/deletes in the ITS region. The phylogenetic analysis indicated that those four strains represent a novel species of Hanseniaspora, for which the names Hanseniaspora terricola sp. nov. (holotype CGMCC 2.6175T; MycoBank MB 834591) is proposed. The other four strains belonging to H. taiwanica produce spherical, void or fusiform ascospores, which differ from the original description that ascospores are absent.

WIPI β-propellers in autophagy-related diseases and longevity

2013 ◽  
Vol 41 (4) ◽  
pp. 962-967 ◽  
Author(s):  
Daniela Bakula ◽  
Zsuzsanna Takacs ◽  
Tassula Proikas-Cezanne
Keyword(s):  
Essential Role ◽  
Mammalian Target Of Rapamycin ◽  
Membrane Vesicles ◽  
Catabolic Pathway ◽  
Autophagosome Formation ◽  
Cytoplasmic Material ◽  
Evolutionarily Conserved ◽  
Initiation Step ◽  
Conserved Amino Acids

Autophagy is a catabolic pathway in which the cell sequesters cytoplasmic material, including long-lived proteins, lipids and organelles, in specialized double-membrane vesicles, called autophagosomes. Subsequently, autophagosomes communicate with the lysosomal compartment and acquire acidic hydrolases for final cargo degradation. This process of partial self-eating secures the survival of eukaryotic cells during starvation periods and is critically regulated by mTORC1 (mammalian target of rapamycin complex 1). Under nutrient-poor conditions, inhibited mTORC1 permits localized PtdIns(3)P production at particular membranes that contribute to autophagosome formation. Members of the human WIPI (WD-repeat protein interacting with phosphoinositides) family fulfil an essential role as PtdIns(3)P effectors at the initiation step of autophagosome formation. In the present article, we discuss the role of human WIPIs in autophagy, and the identification of evolutionarily conserved amino acids of WIPI-1 that confer PtdIns(3)P binding downstream of mTORC1 inhibition. We also discuss the PtdIns(3)P effector function of WIPIs in the context of longevity and autophagy-related human diseases, such as cancer and neurodegeneration.

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