Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase

Abstract DNA ligases, the enzymes responsible for joining breaks in the phosphodiester backbone of DNA during replication and repair, vary considerably in size and structure. The smallest members of this enzyme class carry out their functions with pared-down protein scaffolds comprising only the cor...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Jolyn Pan, Kjersti Lian, Aili Sarre, Hanna-Kirsti S. Leiros, Adele Williamson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/92c6a773ff5d499a8cabcf97ca642d71
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:92c6a773ff5d499a8cabcf97ca642d71
record_format	dspace
spelling	oai:doaj.org-article:92c6a773ff5d499a8cabcf97ca642d712021-12-02T15:14:27ZBacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase10.1038/s41598-021-98155-w2045-2322https://doaj.org/article/92c6a773ff5d499a8cabcf97ca642d712021-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-98155-whttps://doaj.org/toc/2045-2322Abstract DNA ligases, the enzymes responsible for joining breaks in the phosphodiester backbone of DNA during replication and repair, vary considerably in size and structure. The smallest members of this enzyme class carry out their functions with pared-down protein scaffolds comprising only the core catalytic domains. Here we use sequence similarity network analysis of minimal DNA ligases from all biological super kingdoms, to investigate their evolutionary origins, with a particular focus on bacterial variants. This revealed that bacterial Lig C sequences cluster more closely with Eukaryote and Archaeal ligases, while bacterial Lig E sequences cluster most closely with viral sequences. Further refinement of the latter group delineates a cohesive cluster of canonical Lig E sequences that possess a leader peptide, an exclusively bacteriophage group of T7 DNA ligase homologs and a group with high similarity to the Chlorella virus DNA ligase which includes both bacterial and viral enzymes. The structure and function of the bacterially-encoded Chlorella virus homologs were further investigated by recombinantly producing and characterizing, the ATP-dependent DNA ligase from Burkholderia pseudomallei as well as determining its crystal structure in complex with DNA. This revealed that the enzyme has similar activity characteristics to other ATP-dependent DNA ligases, and significant structural similarity to the eukaryotic virus Chlorella virus including the positioning and DNA contacts of the binding latch region. Analysis of the genomic context of the B. pseudomallei ATP-dependent DNA ligase indicates it is part of a lysogenic bacteriophage present in the B. pseudomallei chromosome representing one likely entry point for the horizontal acquisition of ATP-dependent DNA ligases by bacteria.Jolyn PanKjersti LianAili SarreHanna-Kirsti S. LeirosAdele WilliamsonNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jolyn Pan Kjersti Lian Aili Sarre Hanna-Kirsti S. Leiros Adele Williamson Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase
description	Abstract DNA ligases, the enzymes responsible for joining breaks in the phosphodiester backbone of DNA during replication and repair, vary considerably in size and structure. The smallest members of this enzyme class carry out their functions with pared-down protein scaffolds comprising only the core catalytic domains. Here we use sequence similarity network analysis of minimal DNA ligases from all biological super kingdoms, to investigate their evolutionary origins, with a particular focus on bacterial variants. This revealed that bacterial Lig C sequences cluster more closely with Eukaryote and Archaeal ligases, while bacterial Lig E sequences cluster most closely with viral sequences. Further refinement of the latter group delineates a cohesive cluster of canonical Lig E sequences that possess a leader peptide, an exclusively bacteriophage group of T7 DNA ligase homologs and a group with high similarity to the Chlorella virus DNA ligase which includes both bacterial and viral enzymes. The structure and function of the bacterially-encoded Chlorella virus homologs were further investigated by recombinantly producing and characterizing, the ATP-dependent DNA ligase from Burkholderia pseudomallei as well as determining its crystal structure in complex with DNA. This revealed that the enzyme has similar activity characteristics to other ATP-dependent DNA ligases, and significant structural similarity to the eukaryotic virus Chlorella virus including the positioning and DNA contacts of the binding latch region. Analysis of the genomic context of the B. pseudomallei ATP-dependent DNA ligase indicates it is part of a lysogenic bacteriophage present in the B. pseudomallei chromosome representing one likely entry point for the horizontal acquisition of ATP-dependent DNA ligases by bacteria.
format	article
author	Jolyn Pan Kjersti Lian Aili Sarre Hanna-Kirsti S. Leiros Adele Williamson
author_facet	Jolyn Pan Kjersti Lian Aili Sarre Hanna-Kirsti S. Leiros Adele Williamson
author_sort	Jolyn Pan
title	Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase
title_short	Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase
title_full	Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase
title_fullStr	Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase
title_full_unstemmed	Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase
title_sort	bacteriophage origin of some minimal atp-dependent dna ligases: a new structure from burkholderia pseudomallei with striking similarity to chlorella virus ligase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/92c6a773ff5d499a8cabcf97ca642d71
work_keys_str_mv	AT jolynpan bacteriophageoriginofsomeminimalatpdependentdnaligasesanewstructurefromburkholderiapseudomalleiwithstrikingsimilaritytochlorellavirusligase AT kjerstilian bacteriophageoriginofsomeminimalatpdependentdnaligasesanewstructurefromburkholderiapseudomalleiwithstrikingsimilaritytochlorellavirusligase AT ailisarre bacteriophageoriginofsomeminimalatpdependentdnaligasesanewstructurefromburkholderiapseudomalleiwithstrikingsimilaritytochlorellavirusligase AT hannakirstisleiros bacteriophageoriginofsomeminimalatpdependentdnaligasesanewstructurefromburkholderiapseudomalleiwithstrikingsimilaritytochlorellavirusligase AT adelewilliamson bacteriophageoriginofsomeminimalatpdependentdnaligasesanewstructurefromburkholderiapseudomalleiwithstrikingsimilaritytochlorellavirusligase
_version_	1718387583726125056

Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase

Ejemplares similares