Methyltransferases acquired by lactococcal 936-type phage provide protection against restriction endonuclease activity

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dc.contributor.author Murphy, James
dc.contributor.author Klumpp, Jochen
dc.contributor.author Mahony, Jennifer
dc.contributor.author O'Connell Motherway, Mary
dc.contributor.author Nauta, Arjen
dc.contributor.author van Sinderen, Douwe
dc.date.accessioned 2016-01-21T09:31:32Z
dc.date.available 2016-01-21T09:31:32Z
dc.date.issued 2014-10-01
dc.identifier.citation MURPHY, J., KLUMPP, J., MAHONY, J., O’CONNELL-MOTHERWAY, M., NAUTA, A. & VAN SINDEREN, D. 2014. Methyltransferases acquired by lactococcal 936-type phage provide protection against restriction endonuclease activity. BMC Genomics, 15:183, 1-11. http://dx.doi.org/10.1186/1471-2164-15-831 en
dc.identifier.volume 15 en
dc.identifier.startpage 1 en
dc.identifier.endpage 11 en
dc.identifier.issn 1471-2164
dc.identifier.uri http://hdl.handle.net/10468/2205
dc.identifier.doi 10.1186/1471-2164-15-831
dc.description.abstract BACKGROUND: So-called 936-type phages are among the most frequently isolated phages in dairy facilities utilising Lactococcus lactis starter cultures. Despite extensive efforts to control phage proliferation and decades of research, these phages continue to negatively impact cheese production in terms of the final product quality and consequently, monetary return. RESULTS: Whole genome sequencing and in silico analysis of three 936-type phage genomes identified several putative (orphan) methyltransferase (MTase)-encoding genes located within the packaging and replication regions of the genome. Utilising SMRT sequencing, methylome analysis was performed on all three phages, allowing the identification of adenine modifications consistent with N-6 methyladenine sequence methylation, which in some cases could be attributed to these phage-encoded MTases. Heterologous gene expression revealed that M.Phi145I/M.Phi93I and M.Phi93DAM, encoded by genes located within the packaging module, provide protection against the restriction enzymes HphI and DpnII, respectively, representing the first functional MTases identified in members of 936-type phages. CONCLUSIONS: SMRT sequencing technology enabled the identification of the target motifs of MTases encoded by the genomes of three lytic 936-type phages and these MTases represent the first functional MTases identified in this species of phage. The presence of these MTase-encoding genes on 936-type phage genomes is assumed to represent an adaptive response to circumvent host encoded restriction-modification systems thereby increasing the fitness of the phages in a dynamic dairy environment. en
dc.description.sponsorship Science Foundation Ireland (SFI Investigator award (13/IA/1953, 08/IN.1/B1909)); Irish Research Council (Enterprise Partnership Scheme postgraduate scholarship) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Biomed Central Ltd. en
dc.rights © 2014 Murphy et al.; licensee BioMed Central Ltd., 2014. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. en
dc.rights.uri http://creativecommons.org/licenses/by/4.0/ en
dc.subject Lactococcus lactis en
dc.subject Bacteriophage en
dc.subject Methylome en
dc.subject Restriction modification en
dc.subject SMRT sequencing en
dc.subject Bacillus subtilis phages en
dc.subject Bacteriophage resistance en
dc.subject DNA methyltransferases en
dc.subject Functional analysis en
dc.subject Single molecule en
dc.subject Lactis phages en
dc.subject Genes en
dc.subject System en
dc.subject Methylation en
dc.subject Evolution en
dc.title Methyltransferases acquired by lactococcal 936-type phage provide protection against restriction endonuclease activity en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Douwe van Sinderen, Microbiology, University College Cork, Cork, Ireland. +353-21-490-1365 Email: d.vansinderen@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.contributor.funder Irish Research Council for Science Engineering and Technology en
dc.contributor.funder Science Foundation Ireland en
dc.description.status Peer reviewed en
dc.identifier.journaltitle BMC Genomics en
dc.internal.copyrightchecked Open Access articles licensed via CC-BY 4.0 with UCC affiliated authors. Uploaded Jan 2016. en
dc.internal.IRISemailaddress d.vansinderen@ucc.ie en
dc.identifier.articleid 831


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© 2014 Murphy et al.; licensee BioMed Central Ltd., 2014. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. Except where otherwise noted, this item's license is described as © 2014 Murphy et al.; licensee BioMed Central Ltd., 2014. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
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