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dc.contributor.authorSerres, Margrethe H.  Concept link
dc.contributor.authorRiley, Monica  Concept link
dc.date.accessioned2005-11-15T20:35:21Z
dc.date.available2005-11-15T20:35:21Z
dc.date.issued2005-03-09
dc.identifier.citationBMC Genomics 6 (2005): 33en
dc.identifier.urihttps://hdl.handle.net/1912/119
dc.description© 2005 Serres and Riley. This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The definitive version was published in BMC Genomics 6 (2005): 33, doi:10.1186/1471-2164-6-33.
dc.description.abstractBackground: Escherichia coli a model organism provides information for annotation of other genomes. Our analysis of its genome has shown that proteins encoded by fused genes need special attention. Such composite (multimodular) proteins consist of two or more components (modules) encoding distinct functions. Multimodular proteins have been found to complicate both annotation and generation of sequence similar groups. Previous work overstated the number of multimodular proteins in E. coli. This work corrects the identification of modules by including sequence information from proteins in 50 sequenced microbial genomes. Results: Multimodular E. coli K-12 proteins were identified from sequence similarities between their component modules and non-fused proteins in 50 genomes and from the literature. We found 109 multimodular proteins in E. coli containing either two or three modules. Most modules had standalone sequence relatives in other genomes. The separated modules together with all the single (un-fused) proteins constitute the sum of all unimodular proteins of E. coli. Pairwise sequence relationships among all E. coli unimodular proteins generated 490 sequence similar, paralogous groups. Groups ranged in size from 92 to 2 members and had varying degrees of relatedness among their members. Some E. coli enzyme groups were compared to homologs in other bacterial genomes. Conclusion: The deleterious effects of multimodular proteins on annotation and on the formation of groups of paralogs are emphasized. To improve annotation results, all multimodular proteins in an organism should be detected and when known each function should be connected with its location in the sequence of the protein. When transferring functions by sequence similarity, alignment locations must be noted, particularly when alignments cover only part of the sequences, in order to enable transfer of the correct function. Separating multimodular proteins into module units makes it possible to generate protein groups related by both sequence and function, avoiding mixing of unrelated sequences. Organisms differ in sizes of groups of sequence-related proteins. A sample comparison of orthologs to selected E. coli paralogous groups correlates with known physiological and taxonomic relationships between the organisms.en
dc.description.sponsorshipThe research was supported by the Office of Science (BER), U.S. Department of Energy, Grant No. DE-FG02-01ER63202 and by National Aeronautics and Space Administration Astrobiology grant NCC2-1054.en
dc.format.extent382815 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen
dc.publisherBioMed Centralen
dc.relation.urihttps://doi.org/10.1186/1471-2164-6-33
dc.rightsAttribution 2.0 Generic*
dc.rights.urihttp://creativecommons.org/licenses/by/2.0*
dc.subjectEscherichia colien
dc.subjectMultimodular proteinsen
dc.titleGene fusions and gene duplications : relevance to genomic annotation and functional analysisen
dc.typeArticleen
dc.identifier.doi10.1186/1471-2164-6-33


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