scholarly journals Ensembles from ordered and disordered proteins reveal similar structural constraints during evolution

2018 ◽  
Author(s):  
Julia Marchetti ◽  
Alexander Miguel Monzon ◽  
Silvio C.E. Tosatto ◽  
Gustavo Parisi ◽  
María Silvina Fornasari
Keyword(s):  
Protein Function ◽  
Relevant Information ◽  
Biological Information ◽  
Disordered Proteins ◽  
Evolutionary Information ◽  
Structural Constraints ◽  
Biologically Relevant ◽  
Conformational Ensembles ◽  
Residue Contacts ◽  
Constrained Model

AbstractInter-residue contacts determine the structural properties for each conformer in the ensembles describing the native state of proteins. Structural constraints during evolution could then provide biologically relevant information about the conformational ensembles and their relationship with protein function. Here, we studied the proportion of sites evolving under structural constraints in two very different types of ensembles, those coming from ordered or disordered proteins. Using a structurally constrained model of protein evolution we found that both types of ensembles show comparable, near 40%, number of positions evolving under structural constraints. Among these sites, ~68% are in disordered regions and ~57% of them show long-range inter-residue contacts. Also, we found that disordered ensembles are redundant in reference to their structurally constrained evolutionary information and could be described on average with ~11 conformers. Despite the different complexity of the studied ensembles and proteins, the similar constraints reveal a comparable level of selective pressure to maintain their biological functions. These results highlight the importance of the evolutionary information to recover meaningful biological information to further characterize conformational ensembles.

EzEditor: a versatile sequence alignment editor for both rRNA- and protein-coding genes

2014 ◽  
Vol 64 (Pt_2) ◽  
pp. 689-691 ◽  
Author(s):  
Yoon-Seong Jeon ◽  
Kihyun Lee ◽  
Sang-Cheol Park ◽  
Bong-Soo Kim ◽  
Yong-Joon Cho ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Dna Sequences ◽  
Relevant Information ◽  
Biological Information ◽  
Sequence Alignments ◽  
Protein Coding ◽  
Structure Information ◽  
Biologically Relevant ◽  
Molecular Sequence ◽  
Protein Coding Genes

EzEditor is a Java-based molecular sequence editor allowing manipulation of both DNA and protein sequence alignments for phylogenetic analysis. It has multiple features optimized to connect initial computer-generated multiple alignment and subsequent phylogenetic analysis by providing manual editing with reference to biological information specific to the genes under consideration. It provides various functionalities for editing rRNA alignments using secondary structure information. In addition, it supports simultaneous editing of both DNA sequences and their translated protein sequences for protein-coding genes. EzEditor is, to our knowledge, the first sequence editing software designed for both rRNA- and protein-coding genes with the visualization of biologically relevant information and should be useful in molecular phylogenetic studies. EzEditor is based on Java, can be run on all major computer operating systems and is freely available from http://sw.ezbiocloud.net/ezeditor/.

scholarly journals Natural visual cues eliciting predator avoidance in fiddler crabs

2011 ◽  
Vol 278 (1724) ◽  
pp. 3584-3592 ◽  
Author(s):  
Jochen Smolka ◽  
Jochen Zeil ◽  
Jan M. Hemmi
Keyword(s):  
Information Processing ◽  
Predator Avoidance ◽  
Visual Cues ◽  
Video Recording ◽  
Relevant Information ◽  
Visual Signals ◽  
Biological Information ◽  
Fiddler Crabs ◽  
Daily Lives ◽  
Biologically Relevant

To efficiently provide an animal with relevant information, the design of its visual system should reflect the distribution of natural signals and the animal's tasks. In many behavioural contexts, however, we know comparatively little about the moment-to-moment information-processing challenges animals face in their daily lives. In predator avoidance, for instance, we lack an accurate description of the natural signal stream and its value for risk assessment throughout the prey's defensive behaviour. We characterized the visual signals generated by real, potentially predatory events by video-recording bird approaches towards an Uca vomeris colony. Using four synchronized cameras allowed us to simultaneously monitor predator avoidance responses of crabs. We reconstructed the signals generated by dangerous and non-dangerous flying animals, identified the cues that triggered escape responses and compared them with those triggering responses to dummy predators. Fiddler crabs responded to a combination of multiple visual cues (including retinal speed, elevation and visual flicker) that reflect the visual signatures of distinct bird and insect behaviours. This allowed crabs to discriminate between dangerous and non-dangerous events. The results demonstrate the importance of measuring natural sensory signatures of biologically relevant events in order to understand biological information processing and its effects on behavioural organization.

scholarly journals Biological information: why we need a good measure and the challenges ahead

2013 ◽  
Vol 3 (6) ◽  
pp. 20130030 ◽  
Author(s):  
Minus van Baalen
Keyword(s):  
Information Theory ◽  
Temporal Dynamics ◽  
Relevant Information ◽  
Biological Information ◽  
Evolutionary Information ◽  
Ecological Processes ◽  
Starting Point ◽  
Leibler Divergence ◽  
Entropy Measures ◽  
Spatio Temporal

Evolution can be characterized as a process that shapes and maintains information across generations. It is also widely acknowledged that information may play a pivotal role in many other ecological processes. Most of the ecologically relevant information (and some important evolutionary information too) is of a very subjective and analogue kind: individuals use cues that may carry information useful only to them but not to others. This is a problem because most information theory has been developed for objective and discrete information. Can information theory be extended to this theory to incorporate multiple forms of information, each with its own (physical) carriers and dynamics? Here, I will not review all the possible roles that information can play, but rather what conditions an appropriate theory should satisfy. The most promising starting point is provided by entropy measures of conditional probabilities (using the so-called Kullback–Leibler divergence), allowing an assessment of how acquiring information can lead to an increase in fitness. It is irrelevant (to a certain extent) where the information comes from—genes, experience or culture—but it is important to realize that information is not merely subjective but its value should be evaluated in fitness terms, and it is here that evolutionary theory has an enormous potential. A number of important stumbling points remain, however; namely, the identification of whose fitness it concerns and what role the spatio-temporal dynamics plays (which is tightly linked to the nature of the physical carriers of the information and the processes that impact on it).

scholarly journals Intrinsically disordered protein ensembles shape evolutionary rates revealing conformational patterns

2020 ◽  
Author(s):  
Nicolas Palopoli ◽  
Julia Marchetti ◽  
Alexander M. Monzon ◽  
Diego J. Zea ◽  
Silvio C.E. Tosatto ◽  
...  
Keyword(s):  
Structure Function ◽  
Intrinsically Disordered Proteins ◽  
Evolutionary Rate ◽  
Evolutionary Rates ◽  
Disordered Proteins ◽  
Structural Constraints ◽  
Rate Heterogeneity ◽  
Intrinsically Disordered ◽  
Residue Contacts ◽  
Conformational Diversity

AbstractIntrinsically disordered proteins (IDPs) lack stable tertiary structure under physiological conditions. The unique composition and complex dynamical behaviour of IDPs make them a challenge for structural biology and molecular evolution studies. Using NMR ensembles, we found that IDPs evolve under a strong site-specific evolutionary rate heterogeneity, mainly originated by different constraints derived from their inter-residue contacts. Evolutionary rate profiles correlate with the experimentally observed conformational diversity of the protein, allowing the description of different conformational patterns possibly related to their structure-function relationships. The correlation between evolutionary rates and contact information improves when structural information is taken not from any individual conformer or the whole ensemble, but from combining a limited number of conformers. Our results suggest that residue contacts in disordered regions constrain evolutionary rates to conserve the dynamic behaviour of the ensemble and that evolutionary rates can be used as a proxy for the conformational diversity of IDPs.Significance StatementIntrinsically disordered proteins (IDPs) challenge the structure-function relationship paradigm. In this work we found that individual sites of IDPs evolve under a strong rate heterogeneity, mainly due to the structural constraints imposed by contacts between their residues. This can be better explained if the contacts are taken from selected subsets of their alternative native conformations, rather than from individual conformations or the whole native ensemble. From an evolutionary point of view, this result indicates that experimentally-based ensembles are redundant. We also observed that the evolutionary rates follow the structural variability between conformers, unveiling conformational preferences. Our results set the stage for establishing novel evolutionary-based methods to study IDP ensembles.

scholarly journals NoRCE: non-coding RNA sets cis enrichment tool

2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Gulden Olgun ◽  
Afshan Nabi ◽  
Oznur Tastan
Keyword(s):  
Expression Patterns ◽  
Target Prediction ◽  
Enrichment Analysis ◽  
Fruit Fly ◽  
Relevant Information ◽  
R Package ◽  
Data Repository ◽  
Biologically Relevant ◽  
Gene Sets ◽  
Data Files

Abstract Background While some non-coding RNAs (ncRNAs) are assigned critical regulatory roles, most remain functionally uncharacterized. This presents a challenge whenever an interesting set of ncRNAs needs to be analyzed in a functional context. Transcripts located close-by on the genome are often regulated together. This genomic proximity on the sequence can hint at a functional association. Results We present a tool, NoRCE, that performs cis enrichment analysis for a given set of ncRNAs. Enrichment is carried out using the functional annotations of the coding genes located proximal to the input ncRNAs. Other biologically relevant information such as topologically associating domain (TAD) boundaries, co-expression patterns, and miRNA target prediction information can be incorporated to conduct a richer enrichment analysis. To this end, NoRCE includes several relevant datasets as part of its data repository, including cell-line specific TAD boundaries, functional gene sets, and expression data for coding & ncRNAs specific to cancer. Additionally, the users can utilize custom data files in their investigation. Enrichment results can be retrieved in a tabular format or visualized in several different ways. NoRCE is currently available for the following species: human, mouse, rat, zebrafish, fruit fly, worm, and yeast. Conclusions NoRCE is a platform-independent, user-friendly, comprehensive R package that can be used to gain insight into the functional importance of a list of ncRNAs of any type. The tool offers flexibility to conduct the users’ preferred set of analyses by designing their own pipeline of analysis. NoRCE is available in Bioconductor and https://github.com/guldenolgun/NoRCE.

scholarly journals Exploring Curated Conformational Ensembles of Intrinsically Disordered Proteins in the Protein Ensemble Database

2021 ◽  
Vol 1 (7) ◽  
Author(s):  
Federica Quaglia ◽  
Tamas Lazar ◽  
András Hatos ◽  
Peter Tompa ◽  
Damiano Piovesan ◽  
...  
Keyword(s):  
Intrinsically Disordered Proteins ◽  
Disordered Proteins ◽  
Conformational Ensembles ◽  
Intrinsically Disordered

scholarly journals Embeddings from deep learning transfer GO annotations beyond homology

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Maria Littmann ◽  
Michael Heinzinger ◽  
Christian Dallago ◽  
Tobias Olenyi ◽  
Burkhard Rost
Keyword(s):  
Protein Function ◽  
Protein Sequences ◽  
Language Models ◽  
Evolutionary Information ◽  
Pairwise Sequence Identity ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Sequence Identity ◽  
Experimental Function ◽  
Go Terms

AbstractKnowing protein function is crucial to advance molecular and medical biology, yet experimental function annotations through the Gene Ontology (GO) exist for fewer than 0.5% of all known proteins. Computational methods bridge this sequence-annotation gap typically through homology-based annotation transfer by identifying sequence-similar proteins with known function or through prediction methods using evolutionary information. Here, we propose predicting GO terms through annotation transfer based on proximity of proteins in the SeqVec embedding rather than in sequence space. These embeddings originate from deep learned language models (LMs) for protein sequences (SeqVec) transferring the knowledge gained from predicting the next amino acid in 33 million protein sequences. Replicating the conditions of CAFA3, our method reaches an Fmax of 37 ± 2%, 50 ± 3%, and 57 ± 2% for BPO, MFO, and CCO, respectively. Numerically, this appears close to the top ten CAFA3 methods. When restricting the annotation transfer to proteins with < 20% pairwise sequence identity to the query, performance drops (Fmax BPO 33 ± 2%, MFO 43 ± 3%, CCO 53 ± 2%); this still outperforms naïve sequence-based transfer. Preliminary results from CAFA4 appear to confirm these findings. Overall, this new concept is likely to change the annotation of proteins, in particular for proteins from smaller families or proteins with intrinsically disordered regions.

scholarly journals Co-Evolution of Intrinsically Disordered Proteins with Folded Partners Witnessed by Evolutionary Couplings

2018 ◽  
Vol 19 (11) ◽  
pp. 3315 ◽  
Author(s):  
Rita Pancsa ◽  
Fruzsina Zsolyomi ◽  
Peter Tompa
Keyword(s):  
Large Scale ◽  
Intrinsically Disordered Proteins ◽  
Protein Structures ◽  
Disordered Proteins ◽  
Cellular Interaction ◽  
Structural Constraints ◽  
Protein Residues ◽  
Intrinsically Disordered ◽  
Evolutionary Changes ◽  
Folded Proteins

Although improved strategies for the detection and analysis of evolutionary couplings (ECs) between protein residues already enable the prediction of protein structures and interactions, they are mostly restricted to conserved and well-folded proteins. Whereas intrinsically disordered proteins (IDPs) are central to cellular interaction networks, due to the lack of strict structural constraints, they undergo faster evolutionary changes than folded domains. This makes the reliable identification and alignment of IDP homologs difficult, which led to IDPs being omitted in most large-scale residue co-variation analyses. By preforming a dedicated analysis of phylogenetically widespread bacterial IDP–partner interactions, here we demonstrate that partner binding imposes constraints on IDP sequences that manifest in detectable interprotein ECs. These ECs were not detected for interactions mediated by short motifs, rather for those with larger IDP–partner interfaces. Most identified coupled residue pairs reside close (<10 Å) to each other on the interface, with a third of them forming multiple direct atomic contacts. EC-carrying interfaces of IDPs are enriched in negatively charged residues, and the EC residues of both IDPs and partners preferentially reside in helices. Our analysis brings hope that IDP–partner interactions difficult to study could soon be successfully dissected through residue co-variation analysis.

scholarly journals Impact of fluorescent protein fusions on the bacterial flagellar motor

2017 ◽  
Author(s):  
M Heo ◽  
AL Nord ◽  
D Chamousset ◽  
E van Rijn ◽  
HJE Beaumont ◽  
...  
Keyword(s):  
Side Effects ◽  
Protein Function ◽  
Fusion Proteins ◽  
Fluorescent Proteins ◽  
Protein Complexes ◽  
Switching Frequency ◽  
Flagellar Motor ◽  
Internal Dynamics ◽  
Biologically Relevant ◽  
Bacterial Flagellar Motor

AbstractFluorescent fusion proteins open a direct and unique window onto protein function. However, they also introduce the risk of perturbation of the function of the native protein. Successful applications of fluorescent fusions therefore rely on a careful assessment and minimization of the side effects. Such insight, however, is still lacking for many applications of fluorescent fusions. This is particularly relevant in the study of the internal dynamics of motor protein complexes, where both the chemical and mechanical reaction coordinates can be affected. Fluorescent proteins fused to thestatorof the bacterial flagellar motor (BFM) complex have previously been used to successfully unveil the internal subunit dynamics of the motor. Here we report the effects of three different fluorescent proteins fused to the stator, all of which altered BFM behavior. The torque generated by individual stators was reduced while their stoichiometry in the complex remained unaffected. MotB fusions decreased the rotation-direction switching frequency of single motors and induced a novel BFM behavior: a bias-dependent asymmetry in the speed attained in the two rotation directions. All these effects could be mitigated by the insertion of a linker at the fusion point. These findings provide a quantitative account of the effects of fluorescent fusions on BFM dynamics and their alleviation—new insights that advance the use of fluorescent fusions to probe the dynamics of protein complexes.Author summaryMuch of what is known about the biology of proteins was discovered by fusing them to fluorescent proteins that allow detection of their location. But the label comes at a cost: the presence of the tag can alter the behavior of the protein of interest in unforeseen, yet biologically relevant ways. These side effects limit the depth to which fluorescent proteins can be used to probe protein function. One of the systems that has been successfully studied with fluorescent fusions for which these effects have not been addressed are dynamic protein complexes that carry out mechanical work. We examined how fluorescent proteins fused to a component of the bacterial flagellar motor complex impacts its function. Our findings show that the fusion proteins altered biologically relevant dynamical properties of the motor, including induction of a novel mechanical behavior, and demonstrate an approach to alleviate this. These results advance our ability to dissect the bacterial flagellar motor, and the internal dynamics of protein complexes in general, with fluorescent fusion proteins while causing minimal perturbation.

scholarly journals Noise matters: elephants show risk-avoidance behaviour in response to human-generated seismic cues

2021 ◽  
Vol 288 (1953) ◽  
pp. 20210774
Author(s):  
Beth Mortimer ◽  
James A. Walker ◽  
David S. Lolchuragi ◽  
Michael Reinwald ◽  
David Daballen
Keyword(s):  
Seismic Noise ◽  
Information Transfer ◽  
Conservation Management ◽  
Sensory Ecology ◽  
Loxodonta Africana ◽  
Relevant Information ◽  
African Elephants ◽  
Risk Avoidance ◽  
Biologically Relevant ◽  
Seismic Vibrations

African elephants ( Loxodonta africana ) use many sensory modes to gather information about their environment, including the detection of seismic, or ground-based, vibrations. Seismic information is known to include elephant-generated signals, but also potentially encompasses biotic cues that are commonly referred to as ‘noise’. To investigate seismic information transfer in elephants beyond communication, here we tested the hypothesis that wild elephants detect and discriminate between seismic vibrations that differ in their noise types, whether elephant- or human-generated. We played three types of seismic vibrations to elephants: seismic recordings of elephants (elephant-generated), white noise (human-generated) and a combined track (elephant- and human-generated). We found evidence of both detection of seismic noise and discrimination between the two treatments containing human-generated noise. In particular, we found evidence of retreat behaviour, where seismic tracks with human-generated noise caused elephants to move further away from the trial location. We conclude that seismic noise are cues that contain biologically relevant information for elephants that they can associate with risk. This expands our understanding of how elephants use seismic information, with implications for elephant sensory ecology and conservation management.

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