Widespread evolutionary crosstalk among protein domains in the context of multi- domain proteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00493595" target="_blank" >RIV/61388963:_____/18:00493595 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11320/18:10377763 RIV/00216208:11310/18:10377763

Výsledek na webu

<a href="https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0203085" target="_blank" >https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0203085</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1371/journal.pone.0203085" target="_blank" >10.1371/journal.pone.0203085</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Widespread evolutionary crosstalk among protein domains in the context of multi- domain proteins

Popis výsledku v původním jazyce

Domains are distinct units within proteins that typically can fold independently into recognizable three-dimensional structures to facilitate their functions. The structural and functional independence of protein domains is reflected by their apparent modularity in the context of multi-domain proteins. In this work, we examined the coupling of evolution of domain sequences co-occurring within multi-domain proteins to see if it proceeds independently, or in a coordinated manner. We used continuous information theory measures to assess the extent of correlated mutations among domains in multi-domain proteins from organisms across the tree of life. In all multi-domain architectures we examined, domains co-occurring within protein sequences had to some degree undergone concerted evolution. This finding challenges the notion of complete modularity and independence of protein domains, providing new perspective on the evolution of protein sequence and function.

Název v anglickém jazyce

Widespread evolutionary crosstalk among protein domains in the context of multi- domain proteins

Popis výsledku anglicky

Domains are distinct units within proteins that typically can fold independently into recognizable three-dimensional structures to facilitate their functions. The structural and functional independence of protein domains is reflected by their apparent modularity in the context of multi-domain proteins. In this work, we examined the coupling of evolution of domain sequences co-occurring within multi-domain proteins to see if it proceeds independently, or in a coordinated manner. We used continuous information theory measures to assess the extent of correlated mutations among domains in multi-domain proteins from organisms across the tree of life. In all multi-domain architectures we examined, domains co-occurring within protein sequences had to some degree undergone concerted evolution. This finding challenges the notion of complete modularity and independence of protein domains, providing new perspective on the evolution of protein sequence and function.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LM2015047" target="_blank" >LM2015047: Česká národní infrastruktura pro biologická data</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2018

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

PLoS ONE

ISSN

1932-6203

e-ISSN

—

Svazek periodika

13

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

—

Kód UT WoS článku

000443374400020

EID výsledku v databázi Scopus

2-s2.0-85052993774