Analysis of the distribution and evolution of the ATP-dependent DNA ligases of bacteria delineates a distinct phylogenetic group 'Lig E'

Williamson, A; Hjerde, E; Kahlke, T

Analysis of the distribution and evolution of the ATP-dependent DNA ligases of bacteria delineates a distinct phylogenetic group 'Lig E'

Williamson, A Hjerde, E Kahlke, T

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Publication Type:: Journal Article
Citation:: Molecular Microbiology, 2016, 99 (2), pp. 274 - 290
Issue Date:: 2016-01-01

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Field	Value	Language
dc.contributor.author	Williamson, A	en_US
dc.contributor.author	Hjerde, E	en_US
dc.contributor.author	Kahlke, T https://orcid.org/0000-0002-9762-6573	en_US
dc.date.available	2015-09-23	en_US
dc.date.issued	2016-01-01	en_US
dc.identifier.citation	Molecular Microbiology, 2016, 99 (2), pp. 274 - 290	en_US
dc.identifier.issn	0950-382X	en_US
dc.identifier.uri	http://hdl.handle.net/10453/90305
dc.description.abstract	© 2016 John Wiley & Sons Ltd. Prior to the discovery of a minimal ATP-dependent DNA ligase in Haemophilus influenzae, bacteria were thought to only possess a NAD-dependent ligase, which was involved in sealing of Okazaki fragments. We now know that a diverse range of bacterial species possess up to six of these accessory bacterial ATP-dependent DNA ligases (b-ADLs), which vary in size and enzymatic domain associations. Here we compare the domain structure of different types of b-ADLs and investigate their distribution among the bacterial domain to describe possible evolutionary trajectories that gave rise to the sequence and structural diversity of these enzymes. Previous biochemical and genetic analyses have delineated three main classes of these enzymes: Lig B, Lig C and Lig D, which appear to have descended from a common ancestor within the bacterial domain. In the present study, we delineate a fourth group of b-ADLs, Lig E, which possesses a number of unique features at the primary and tertiary structural levels. The biochemical characteristics, domain structure and inferred extracellular location sets this group apart from the other b-ADLs. The results presented here indicate that the Lig E type ligases were horizontally transferred into bacteria in a separate event from other b-ADLs possibly from a bacteriophage. Some bacteria possess accessory ATP-dependent DNA ligases (ADLs) which vary in size and the composition of enzymatic domains and appear to have been horizontally acquired. Our analysis of the distribution and phylogeny of these bacterial ADLs suggests that types Lig B, Lig C and Lig D have descended from a common ancestor within the bacterial domain, while Lig E was transferred in a separate event, possibly from a bacteriophage.	en_US
dc.relation.ispartof	Molecular Microbiology	en_US
dc.relation.isbasedon	10.1111/mmi.13229	en_US
dc.subject.classification	Microbiology	en_US
dc.subject.mesh	Bacteria	en_US
dc.subject.mesh	DNA Ligases	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	Adenosine Triphosphate	en_US
dc.subject.mesh	Evolution, Molecular	en_US
dc.subject.mesh	Phylogeny	en_US
dc.subject.mesh	DNA Ligase ATP	en_US
dc.title	Analysis of the distribution and evolution of the ATP-dependent DNA ligases of bacteria delineates a distinct phylogenetic group 'Lig E'	en_US
dc.type	Journal Article
utslib.citation.volume	2	en_US
utslib.citation.volume	99	en_US
utslib.for	0602 Ecology	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	07 Agricultural and Veterinary Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - C3 - Climate Change Cluster
utslib.copyright.status	closed_access
pubs.issue	2	en_US
pubs.publication-status	Published	en_US
pubs.volume	99	en_US

Abstract:

© 2016 John Wiley & Sons Ltd. Prior to the discovery of a minimal ATP-dependent DNA ligase in Haemophilus influenzae, bacteria were thought to only possess a NAD-dependent ligase, which was involved in sealing of Okazaki fragments. We now know that a diverse range of bacterial species possess up to six of these accessory bacterial ATP-dependent DNA ligases (b-ADLs), which vary in size and enzymatic domain associations. Here we compare the domain structure of different types of b-ADLs and investigate their distribution among the bacterial domain to describe possible evolutionary trajectories that gave rise to the sequence and structural diversity of these enzymes. Previous biochemical and genetic analyses have delineated three main classes of these enzymes: Lig B, Lig C and Lig D, which appear to have descended from a common ancestor within the bacterial domain. In the present study, we delineate a fourth group of b-ADLs, Lig E, which possesses a number of unique features at the primary and tertiary structural levels. The biochemical characteristics, domain structure and inferred extracellular location sets this group apart from the other b-ADLs. The results presented here indicate that the Lig E type ligases were horizontally transferred into bacteria in a separate event from other b-ADLs possibly from a bacteriophage. Some bacteria possess accessory ATP-dependent DNA ligases (ADLs) which vary in size and the composition of enzymatic domains and appear to have been horizontally acquired. Our analysis of the distribution and phylogeny of these bacterial ADLs suggests that types Lig B, Lig C and Lig D have descended from a common ancestor within the bacterial domain, while Lig E was transferred in a separate event, possibly from a bacteriophage.

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http://hdl.handle.net/10453/90305