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dc.contributor.authorKamneva, Olga K.
dc.contributor.authorPoudel, Saroj
dc.contributor.authorWard, Naomi L.
dc.date.accessioned2015-11-18T19:25:18Z
dc.date.available2015-11-18T19:25:18Z
dc.date.issued2015-06
dc.identifier.citationKamneva, Olga K., Saroj Poudel, and Naomi L. Ward. "Proteins Related to the Type I Secretion System Are Associated with Secondary SecA_DEAD Domain Proteins in Some Species of Planctomycetes, Verrucomicrobia, Proteobacteria, Nitrospirae and Chlorobi." PLoS One 10, no. 6 (June 2015): e0129066. DOI:https://dx.doi.org/10.1371/journal.pone.0129066.en_US
dc.identifier.issn1932-6203
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/9383
dc.description.abstractA number of bacteria belonging to the PVC (Planctomycetes-Verrucomicrobia-Chlamydiae) super-phylum contain unusual ribosome-bearing intracellular membranes. The evolutionary origins and functions of these membranes are unknown. Some proteins putatively associated with the presence of intracellular membranes in PVC bacteria contain signal peptides. Signal peptides mark proteins for translocation across the cytoplasmic membrane in prokaryotes, and the membrane of the endoplasmic reticulum in eukaryotes, by highly conserved Sec machinery. This suggests that proteins might be targeted to intracellular membranes in PVC bacteria via the Sec pathway. Here, we show that canonical signal peptides are significantly over-represented in proteins preferentially present in PVC bacteria possessing intracellular membranes, indicating involvement of Sec translocase in their cellular targeting. We also characterized Sec proteins using comparative genomics approaches, focusing on the PVC super-phylum. While we were unable to detect unique changes in Sec proteins conserved among membrane-bearing PVC species, we identified (1) SecA ATPase domain re-arrangements in some Planctomycetes, and (2) secondary SecA_DEAD domain proteins in the genomes of some Planctomycetes, Verrucomicrobia, Proteobacteria, Nitrospirae and Chlorobi. This is the first report of potentially duplicated SecA in Gram-negative bacteria. The phylogenetic distribution of secondary SecA_DEAD domain proteins suggests that the presence of these proteins is not related to the occurrence of PVC endomembranes. Further genomic analysis showed that secondary SecA_DEAD domain proteins are located within genomic neighborhoods that also encode three proteins possessing domains specific for the Type I secretion system.en_US
dc.rightsCC BY 4.0en_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/legalcodeen_US
dc.titleProteins Related to the Type I Secretion System Are Associated with Secondary SecA_DEAD Domain Proteins in Some Species of Planctomycetes, Verrucomicrobia, Proteobacteria, Nitrospirae and Chlorobien_US
dc.typeArticleen_US
mus.citation.extentfirstpagee0129066en_US
mus.citation.issue6en_US
mus.citation.journaltitlePLoS ONEen_US
mus.citation.volume10en_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1371/journal.pone.0129066en_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.departmentComputer Science.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.data.thumbpage11en_US


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