107 research outputs found

    Number of natively unfolded proteins scales with genome size

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    Natively unfolded proteins exist as an ensemble of flexible conformations lacking a well defined tertiary structure along a large portion of their polypeptide chain. Despite the absence of a stable configuration, they are involved in important cellular processes. In this work we used from three indicators of folding status, derived from the analysis of mean packing and mean contact energy of a protein sequence as well as from VSL2, a disorder predictor, and we combined them into a consensus score to identify natively unfolded proteins in several genomes from Archaea, Bacteria and Eukarya. We found a high correlation among the number of predicted natively unfolded proteins and the number of proteins in the genomes. More specifically, the number of natively unfolded proteins scaled with the number of proteins in the genomes, with exponent 1.81 +- 0.10. This scaling law may be important to understand the relation between the number of natively unfolded proteins and their roles in cellular processes.Comment: Submitted to Biophysics and Bioengineering Letters http://padis2.uniroma1.it:81/ojs/index.php/CISB-BB

    Causal influence in linear response models

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    The intuition of causation is so fundamental that almost every research study in life sciences refers to this concept. However a widely accepted formal definition of causal influence between observables is still missing. In the framework of linear Langevin networks without feedbacks (linear response models) we developed a measure of causal influence based on a decomposition of information flows over time. We discuss its main properties and compare it with other information measures like the Transfer Entropy. Finally we outline some difficulties of the extension to a general definition of causal influence for complex systems.Comment: 9 pages, 9 figure

    Bacterial protein interaction networks: connectivity is ruled by gene conservation, essentiality and function

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    Protein-protein interaction (PPI) networks are the backbone of all processes in living cells. In this work we relate conservation, essentiality and functional repertoire of a gene to the connectivity kk of the corresponding protein in the PPI networks. Focusing on a set of 42 bacterial species with reasonably separated evolutionary trajectories, we investigate three issues: i) whether the distribution of connectivity values changes between PPI subnetworks of essential and nonessential genes; ii) how gene conservation, measured both by the evolutionary retention index (ERI) and by evolutionary pressures (evaluated through the ratio Ka/KsK_a/K_s and ENC plots) is related to the the connectivity of the corresponding protein; iii) how PPI connectivities are modulated by evolutionary and functional relationships, as represented by the Clusters of Orthologous Proteins (COGs). We show that conservation, essentiality and functional specialization of genes control in a quite universal way the topology of the emerging bacterial PPI networks. Noteworthy, a structural transition in the network is observed such that, for connectivities k≥40k\ge40, bacterial PPI networks are mostly populated by genes that are conserved, essential and which, in most cases, belong to the COG cluster J, related to ribosomal functions and to the processing of genetic information

    Codon Bias Patterns of E.coliE.coli's Interacting Proteins

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    Synonymous codons, i.e., DNA nucleotide triplets coding for the same amino acid, are used differently across the variety of living organisms. The biological meaning of this phenomenon, known as codon usage bias, is still controversial. In order to shed light on this point, we propose a new codon bias index, CompAICompAI, that is based on the competition between cognate and near-cognate tRNAs during translation, without being tuned to the usage bias of highly expressed genes. We perform a genome-wide evaluation of codon bias for E.coliE.coli, comparing CompAICompAI with other widely used indices: tAItAI, CAICAI, and NcNc. We show that CompAICompAI and tAItAI capture similar information by being positively correlated with gene conservation, measured by ERI, and essentiality, whereas, CAICAI and NcNc appear to be less sensitive to evolutionary-functional parameters. Notably, the rate of variation of tAItAI and CompAICompAI with ERI allows to obtain sets of genes that consistently belong to specific clusters of orthologous genes (COGs). We also investigate the correlation of codon bias at the genomic level with the network features of protein-protein interactions in E.coliE.coli. We find that the most densely connected communities of the network share a similar level of codon bias (as measured by CompAICompAI and tAItAI). Conversely, a small difference in codon bias between two genes is, statistically, a prerequisite for the corresponding proteins to interact. Importantly, among all codon bias indices, CompAICompAI turns out to have the most coherent distribution over the communities of the interactome, pointing to the significance of competition among cognate and near-cognate tRNAs for explaining codon usage adaptation
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