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Parameters of proteome evolution from histograms of amino-acid sequence identities of paralogous proteins

BACKGROUND: The evolution of the full repertoire of proteins encoded in a given genome is mostly driven by gene duplications, deletions, and sequence modifications of existing proteins. Indirect information about relative rates and other intrinsic parameters of these three basic processes is contain...

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Autores principales: Axelsen, Jacob Bock, Yan, Koon-Kiu, Maslov, Sergei
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2246104/
https://www.ncbi.nlm.nih.gov/pubmed/18039386
http://dx.doi.org/10.1186/1745-6150-2-32
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author Axelsen, Jacob Bock
Yan, Koon-Kiu
Maslov, Sergei
author_facet Axelsen, Jacob Bock
Yan, Koon-Kiu
Maslov, Sergei
author_sort Axelsen, Jacob Bock
collection PubMed
description BACKGROUND: The evolution of the full repertoire of proteins encoded in a given genome is mostly driven by gene duplications, deletions, and sequence modifications of existing proteins. Indirect information about relative rates and other intrinsic parameters of these three basic processes is contained in the proteome-wide distribution of sequence identities of pairs of paralogous proteins. RESULTS: We introduce a simple mathematical framework based on a stochastic birth-and-death model that allows one to extract some of this information and apply it to the set of all pairs of paralogous proteins in H. pylori, E. coli, S. cerevisiae, C. elegans, D. melanogaster, and H. sapiens. It was found that the histogram of sequence identities p generated by an all-to-all alignment of all protein sequences encoded in a genome is well fitted with a power-law form ~ p(-γ )with the value of the exponent γ around 4 for the majority of organisms used in this study. This implies that the intra-protein variability of substitution rates is best described by the Gamma-distribution with the exponent α ≈ 0.33. Different features of the shape of such histograms allow us to quantify the ratio between the genome-wide average deletion/duplication rates and the amino-acid substitution rate. CONCLUSION: We separately measure the short-term ("raw") duplication and deletion rates [Formula: see text] , [Formula: see text] which include gene copies that will be removed soon after the duplication event and their dramatically reduced long-term counterparts r(dup), r(del). High deletion rate among recently duplicated proteins is consistent with a scenario in which they didn't have enough time to significantly change their functional roles and thus are to a large degree disposable. Systematic trends of each of the four duplication/deletion rates with the total number of genes in the genome were analyzed. All but the deletion rate of recent duplicates [Formula: see text] were shown to systematically increase with N(genes). Abnormally flat shapes of sequence identity histograms observed for yeast and human are consistent with lineages leading to these organisms undergoing one or more whole-genome duplications. This interpretation is corroborated by our analysis of the genome of Paramecium tetraurelia where the p(-4 )profile of the histogram is gradually restored by the successive removal of paralogs generated in its four known whole-genome duplication events.
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spelling pubmed-22461042008-02-20 Parameters of proteome evolution from histograms of amino-acid sequence identities of paralogous proteins Axelsen, Jacob Bock Yan, Koon-Kiu Maslov, Sergei Biol Direct Research BACKGROUND: The evolution of the full repertoire of proteins encoded in a given genome is mostly driven by gene duplications, deletions, and sequence modifications of existing proteins. Indirect information about relative rates and other intrinsic parameters of these three basic processes is contained in the proteome-wide distribution of sequence identities of pairs of paralogous proteins. RESULTS: We introduce a simple mathematical framework based on a stochastic birth-and-death model that allows one to extract some of this information and apply it to the set of all pairs of paralogous proteins in H. pylori, E. coli, S. cerevisiae, C. elegans, D. melanogaster, and H. sapiens. It was found that the histogram of sequence identities p generated by an all-to-all alignment of all protein sequences encoded in a genome is well fitted with a power-law form ~ p(-γ )with the value of the exponent γ around 4 for the majority of organisms used in this study. This implies that the intra-protein variability of substitution rates is best described by the Gamma-distribution with the exponent α ≈ 0.33. Different features of the shape of such histograms allow us to quantify the ratio between the genome-wide average deletion/duplication rates and the amino-acid substitution rate. CONCLUSION: We separately measure the short-term ("raw") duplication and deletion rates [Formula: see text] , [Formula: see text] which include gene copies that will be removed soon after the duplication event and their dramatically reduced long-term counterparts r(dup), r(del). High deletion rate among recently duplicated proteins is consistent with a scenario in which they didn't have enough time to significantly change their functional roles and thus are to a large degree disposable. Systematic trends of each of the four duplication/deletion rates with the total number of genes in the genome were analyzed. All but the deletion rate of recent duplicates [Formula: see text] were shown to systematically increase with N(genes). Abnormally flat shapes of sequence identity histograms observed for yeast and human are consistent with lineages leading to these organisms undergoing one or more whole-genome duplications. This interpretation is corroborated by our analysis of the genome of Paramecium tetraurelia where the p(-4 )profile of the histogram is gradually restored by the successive removal of paralogs generated in its four known whole-genome duplication events. BioMed Central 2007-11-26 /pmc/articles/PMC2246104/ /pubmed/18039386 http://dx.doi.org/10.1186/1745-6150-2-32 Text en Copyright © 2007 Axelsen et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Axelsen, Jacob Bock
Yan, Koon-Kiu
Maslov, Sergei
Parameters of proteome evolution from histograms of amino-acid sequence identities of paralogous proteins
title Parameters of proteome evolution from histograms of amino-acid sequence identities of paralogous proteins
title_full Parameters of proteome evolution from histograms of amino-acid sequence identities of paralogous proteins
title_fullStr Parameters of proteome evolution from histograms of amino-acid sequence identities of paralogous proteins
title_full_unstemmed Parameters of proteome evolution from histograms of amino-acid sequence identities of paralogous proteins
title_short Parameters of proteome evolution from histograms of amino-acid sequence identities of paralogous proteins
title_sort parameters of proteome evolution from histograms of amino-acid sequence identities of paralogous proteins
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2246104/
https://www.ncbi.nlm.nih.gov/pubmed/18039386
http://dx.doi.org/10.1186/1745-6150-2-32
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