Background Protein domains can be used to study proteome evolution at a coarse scale. In particular, they are found on genomes with notable statistical distributions. It is known that the distribution of domains with a given topology follows a power law. We focus on a further aspect: these distributions, and the number of distinct topologies, follow collective trends, or scaling laws, depending on the total number of domains only, and not on genome-specific features. Results We present a stochastic duplication/innovation model, in the class of the so-called 'Chinese restaurant processes', that explains this observation with two universal parameters, representing a minimal number of domains and the relative weight of innovation to duplication. Furthermore, we study a model variant where new topologies are related to occurrence in genomic data, accounting for fold specificity. Conclusions Both models have general quantitative agreement with data from hundreds of genomes, which indicates that the domains of a genome are built with a combination of specificity and robust self-organizing phenomena. The latter are related to the basic evolutionary 'moves' of duplication and innovation, and give rise to the observed scaling laws, a priori of the specific evolutionary history of a genome. We interpret this as the concurrent effect of neutral and selective drives, which increase duplication and decrease innovation in larger and more complex genomes. The validity of our model would imply that the empirical observation of a small number of folds in nature may be a consequence of their evolution.

Universal features in the genome-level evolution of protein domains / M. Cosentino Lagomarsino, A.L. Sellerio, P.D. Heijning, B.F. Bassetti. - In: GENOME BIOLOGY. - ISSN 1474-760X. - 10:1(2009), pp. R12.R12.1-R12.R12.13.

Universal features in the genome-level evolution of protein domains

M. Cosentino Lagomarsino;B.F. Bassetti
Ultimo
2009

Abstract

Background Protein domains can be used to study proteome evolution at a coarse scale. In particular, they are found on genomes with notable statistical distributions. It is known that the distribution of domains with a given topology follows a power law. We focus on a further aspect: these distributions, and the number of distinct topologies, follow collective trends, or scaling laws, depending on the total number of domains only, and not on genome-specific features. Results We present a stochastic duplication/innovation model, in the class of the so-called 'Chinese restaurant processes', that explains this observation with two universal parameters, representing a minimal number of domains and the relative weight of innovation to duplication. Furthermore, we study a model variant where new topologies are related to occurrence in genomic data, accounting for fold specificity. Conclusions Both models have general quantitative agreement with data from hundreds of genomes, which indicates that the domains of a genome are built with a combination of specificity and robust self-organizing phenomena. The latter are related to the basic evolutionary 'moves' of duplication and innovation, and give rise to the observed scaling laws, a priori of the specific evolutionary history of a genome. We interpret this as the concurrent effect of neutral and selective drives, which increase duplication and decrease innovation in larger and more complex genomes. The validity of our model would imply that the empirical observation of a small number of folds in nature may be a consequence of their evolution.
English
Settore FIS/02 - Fisica Teorica, Modelli e Metodi Matematici
Articolo
Sì, ma tipo non specificato
2009
BioMed Central
10
1
R12
R12.1
R12.13
Periodico con rilevanza internazionale
info:eu-repo/semantics/article
Universal features in the genome-level evolution of protein domains / M. Cosentino Lagomarsino, A.L. Sellerio, P.D. Heijning, B.F. Bassetti. - In: GENOME BIOLOGY. - ISSN 1474-760X. - 10:1(2009), pp. R12.R12.1-R12.R12.13.
none
Prodotti della ricerca::01 - Articolo su periodico
4
262
Article (author)
si
M. Cosentino Lagomarsino, A.L. Sellerio, P.D. Heijning, B.F. Bassetti
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/157091
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