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Bacterial calpains and the evolution of the calpain (C2) family of peptidases.


ABSTRACT: 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.

SUBMITTER: Rawlings ND 

PROVIDER: S-EPMC4631099 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature

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Bacterial calpains and the evolution of the calpain (C2) family of peptidases.

Rawlings Neil D ND  

Biology direct 20151102


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  ...[more]

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