Evolutionary mode for the functional preservation of fast-evolving <italic toggle="yes">Drosophila</italic> telomere capping proteins

DNA end protection is fundamental for the long-term preservation of the genome. In vertebrates the Shelterin protein complex protects telomeric DNA ends, thereby contributing to the maintenance of genome integrity. In the Drosophila genus, this function is thought to be performed by the Terminin com...

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Autores principales:	Balázs Vedelek, Ákos Kovács, Imre M. Boros
Formato:	article
Lenguaje:	EN
Publicado:	The Royal Society 2021
Materias:	Terminin fast evolution Ob-fold Ver Moi DTL Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/121840f875164d53a706decae324b8bd
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spelling	oai:doaj.org-article:121840f875164d53a706decae324b8bd2021-11-17T08:06:15ZEvolutionary mode for the functional preservation of fast-evolving <italic toggle="yes">Drosophila</italic> telomere capping proteins10.1098/rsob.2102612046-2441https://doaj.org/article/121840f875164d53a706decae324b8bd2021-11-01T00:00:00Zhttps://royalsocietypublishing.org/doi/10.1098/rsob.210261https://doaj.org/toc/2046-2441DNA end protection is fundamental for the long-term preservation of the genome. In vertebrates the Shelterin protein complex protects telomeric DNA ends, thereby contributing to the maintenance of genome integrity. In the Drosophila genus, this function is thought to be performed by the Terminin complex, an assembly of fast-evolving subunits. Considering that DNA end protection is fundamental for successful genome replication, the accelerated evolution of Terminin subunits is counterintuitive, as conservation is supposed to maintain the assembly and concerted function of the interacting partners. This problem extends over Drosophila telomere biology and provides insight into the evolution of protein assemblies. In order to learn more about the mechanistic details of this phenomenon we have investigated the intra- and interspecies assemblies of Verrocchio and Modigliani, two Terminin subunits using in vitro assays. Based on our results and on homology-based three-dimensional models for Ver and Moi, we conclude that both proteins contain Ob-fold and contribute to the ssDNA binding of the Terminin complex. We propose that the preservation of Ver function is achieved by conservation of specific amino acids responsible for folding or localized in interacting surfaces. We also provide here the first evidence on Moi DNA binding.Balázs VedelekÁkos KovácsImre M. BorosThe Royal SocietyarticleTermininfast evolutionOb-foldVerMoiDTLBiology (General)QH301-705.5ENOpen Biology, Vol 11, Iss 11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Terminin fast evolution Ob-fold Ver Moi DTL Biology (General) QH301-705.5
spellingShingle	Terminin fast evolution Ob-fold Ver Moi DTL Biology (General) QH301-705.5 Balázs Vedelek Ákos Kovács Imre M. Boros Evolutionary mode for the functional preservation of fast-evolving <italic toggle="yes">Drosophila</italic> telomere capping proteins
description	DNA end protection is fundamental for the long-term preservation of the genome. In vertebrates the Shelterin protein complex protects telomeric DNA ends, thereby contributing to the maintenance of genome integrity. In the Drosophila genus, this function is thought to be performed by the Terminin complex, an assembly of fast-evolving subunits. Considering that DNA end protection is fundamental for successful genome replication, the accelerated evolution of Terminin subunits is counterintuitive, as conservation is supposed to maintain the assembly and concerted function of the interacting partners. This problem extends over Drosophila telomere biology and provides insight into the evolution of protein assemblies. In order to learn more about the mechanistic details of this phenomenon we have investigated the intra- and interspecies assemblies of Verrocchio and Modigliani, two Terminin subunits using in vitro assays. Based on our results and on homology-based three-dimensional models for Ver and Moi, we conclude that both proteins contain Ob-fold and contribute to the ssDNA binding of the Terminin complex. We propose that the preservation of Ver function is achieved by conservation of specific amino acids responsible for folding or localized in interacting surfaces. We also provide here the first evidence on Moi DNA binding.
format	article
author	Balázs Vedelek Ákos Kovács Imre M. Boros
author_facet	Balázs Vedelek Ákos Kovács Imre M. Boros
author_sort	Balázs Vedelek
title	Evolutionary mode for the functional preservation of fast-evolving <italic toggle="yes">Drosophila</italic> telomere capping proteins
title_short	Evolutionary mode for the functional preservation of fast-evolving <italic toggle="yes">Drosophila</italic> telomere capping proteins
title_full	Evolutionary mode for the functional preservation of fast-evolving <italic toggle="yes">Drosophila</italic> telomere capping proteins
title_fullStr	Evolutionary mode for the functional preservation of fast-evolving <italic toggle="yes">Drosophila</italic> telomere capping proteins
title_full_unstemmed	Evolutionary mode for the functional preservation of fast-evolving <italic toggle="yes">Drosophila</italic> telomere capping proteins
title_sort	evolutionary mode for the functional preservation of fast-evolving <italic toggle="yes">drosophila</italic> telomere capping proteins
publisher	The Royal Society
publishDate	2021
url	https://doaj.org/article/121840f875164d53a706decae324b8bd
work_keys_str_mv	AT balazsvedelek evolutionarymodeforthefunctionalpreservationoffastevolvingitalictoggleyesdrosophilaitalictelomerecappingproteins AT akoskovacs evolutionarymodeforthefunctionalpreservationoffastevolvingitalictoggleyesdrosophilaitalictelomerecappingproteins AT imremboros evolutionarymodeforthefunctionalpreservationoffastevolvingitalictoggleyesdrosophilaitalictelomerecappingproteins
_version_	1718425780953808896

Evolutionary mode for the functional preservation of fast-evolving <italic toggle="yes">Drosophila</italic> telomere capping proteins

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