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dc.contributor.author Ravagnani, Adriana
dc.contributor.author Finan, Christopher L.
dc.contributor.author Young, Michael
dc.date.accessioned 2009-09-08T08:33:01Z
dc.date.available 2009-09-08T08:33:01Z
dc.date.issued 2005-03-17
dc.identifier.citation Ravagnani , A , Finan , C L & Young , M 2005 , ' A novel firmicute protein family related to the actinobacterial resuscitation-promoting factors by non-orthologous domain displacement ' BMC Genomics , vol 6 , pp. 39-52 . , 10.1186/1471-2164-6-39 en
dc.identifier.issn 1471-2164
dc.identifier.other PURE: 116257
dc.identifier.other dspace: 2160/2976
dc.identifier.uri http://hdl.handle.net/2160/2976
dc.identifier.uri http://www.biomedcentral.com/1471-2164/6/39 en
dc.description Ravagnani, A., Finan, C. L., Young, M. (2005). A novel firmicute protein family related to the actinobacterial resuscitation-promoting factors by non-orthologous domain displacement.  BMC Genomics, 6, paper 39 Sponsorship: This work was funded by the UK BBSRC. C.L.F. was the grateful recipient of a BBSRC studentship. en
dc.description.abstract Background In Micrococcus luteus growth and resuscitation from starvation-induced dormancy is controlled by the production of a secreted growth factor. This autocrine resuscitation-promoting factor (Rpf) is the founder member of a family of proteins found throughout and confined to the actinobacteria (high G + C Gram-positive bacteria). The aim of this work was to search for and characterise a cognate gene family in the firmicutes (low G + C Gram-positive bacteria) and obtain information about how they may control bacterial growth and resuscitation. Results In silico analysis of the accessory domains of the Rpf proteins permitted their classification into several subfamilies. The RpfB subfamily is related to a group of firmicute proteins of unknown function, represented by YabE of Bacillus subtilis. The actinobacterial RpfB and firmicute YabE proteins have very similar domain structures and genomic contexts, except that in YabE, the actinobacterial Rpf domain is replaced by another domain, which we have called Sps. Although totally unrelated in both sequence and secondary structure, the Rpf and Sps domains fulfil the same function. We propose that these proteins have undergone "non-orthologous domain displacement", a phenomenon akin to "non-orthologous gene displacement" that has been described previously. Proteins containing the Sps domain are widely distributed throughout the firmicutes and they too fall into a number of distinct subfamilies. Comparative analysis of the accessory domains in the Rpf and Sps proteins, together with their weak similarity to lytic transglycosylases, provide clear evidence that they are muralytic enzymes. Conclusions The results indicate that the firmicute Sps proteins and the actinobacterial Rpf proteins are cognate and that they control bacterial culturability via enzymatic modification of the bacterial cell envelope. en
dc.format.extent 13 en
dc.language.iso eng
dc.relation.ispartof BMC Genomics en
dc.title A novel firmicute protein family related to the actinobacterial resuscitation-promoting factors by non-orthologous domain displacement en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1186/1471-2164-6-39
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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