Bacterial calpains and the evolution of the calpain (C2) family of peptidases
Homologues of calpain, often thought to be an essential, cytoplasmic, calcium-dependent cysteine endopeptidase found exclusively in eukaryotes, have been found in bacterial proteomes. The homologues lack calcium-binding sites, have differing domain architectures, and can be secreted or membrane-asso...
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BioMed Central
2015
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4631099/ |
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pubmed-46310992015-11-04 Bacterial calpains and the evolution of the calpain (C2) family of peptidases Rawlings, Neil D. Discovery Notes Homologues of calpain, often thought to be an essential, cytoplasmic, calcium-dependent cysteine endopeptidase found exclusively in eukaryotes, have been found in bacterial proteomes. The homologues lack calcium-binding sites, have differing domain architectures, and can be secreted or membrane-associated. Homologues are rare and occur in a minority of bacterial phyla and often in a minority of species in a genus. However, the differences in domain architecture argue against a recent, horizontal gene transfer from a eukaryote. From analysis of a phylogenetic tree and absence of homologues in archaea, calpains in eukaryotes may be derived from genes horizontally transferred from a bacterium. BioMed Central 2015-11-02 /pmc/articles/PMC4631099/ /pubmed/26527411 http://dx.doi.org/10.1186/s13062-015-0095-0 Text en © Rawlings. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Rawlings, Neil D. |
| spellingShingle |
Rawlings, Neil D. Bacterial calpains and the evolution of the calpain (C2) family of peptidases |
| author_facet |
Rawlings, Neil D. |
| author_sort |
Rawlings, Neil D. |
| title |
Bacterial calpains and the evolution of the calpain (C2) family of peptidases |
| title_short |
Bacterial calpains and the evolution of the calpain (C2) family of peptidases |
| title_full |
Bacterial calpains and the evolution of the calpain (C2) family of peptidases |
| title_fullStr |
Bacterial calpains and the evolution of the calpain (C2) family of peptidases |
| title_full_unstemmed |
Bacterial calpains and the evolution of the calpain (C2) family of peptidases |
| title_sort |
bacterial calpains and the evolution of the calpain (c2) family of peptidases |
| description |
Homologues of calpain, often thought to be an essential, cytoplasmic, calcium-dependent cysteine endopeptidase found exclusively in eukaryotes, have been found in bacterial proteomes. The homologues lack calcium-binding sites, have differing domain architectures, and can be secreted or membrane-associated. Homologues are rare and occur in a minority of bacterial phyla and often in a minority of species in a genus. However, the differences in domain architecture argue against a recent, horizontal gene transfer from a eukaryote. From analysis of a phylogenetic tree and absence of homologues in archaea, calpains in eukaryotes may be derived from genes horizontally transferred from a bacterium. |
| publisher |
BioMed Central |
| publishDate |
2015 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4631099/ |
| _version_ |
1613496627904905216 |