Evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites.
Employing whole-genome analysis we have characterized a large family of genes coding for calpain-related proteins in three kinetoplastid parasites. We have defined a total of 18 calpain-like sequences in Trypanosoma brucei, 27 in Leishmania major, and 24 in Trypanosoma cruzi. Sequence characterizati...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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2005
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| _version_ | 1797073656526929920 |
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| author | Ersfeld, K Barraclough, H Gull, K |
| author_facet | Ersfeld, K Barraclough, H Gull, K |
| author_sort | Ersfeld, K |
| collection | OXFORD |
| description | Employing whole-genome analysis we have characterized a large family of genes coding for calpain-related proteins in three kinetoplastid parasites. We have defined a total of 18 calpain-like sequences in Trypanosoma brucei, 27 in Leishmania major, and 24 in Trypanosoma cruzi. Sequence characterization revealed a well-conserved protease domain in most proteins, although residues critical for catalytic activity were frequently altered. Many of the proteins contain a novel N-terminal sequence motif unique to kinetoplastids. Furthermore, 24 of the sequences contain N-terminal fatty acid acylation motifs indicating association of these proteins with intracellular membranes. This extended family of proteins also includes a group of sequences that completely lack a protease domain but is specifically related to other kinetoplastid calpain-related proteins by a highly conserved N-terminal domain and by genomic organization. All sequences lack the C-terminal calmodulin-related calcium-binding domain typical of most mammalian calpains. Our analysis emphasizes the highly modular structure of calpains and calpain-like proteins, suggesting that they are involved in diverse cellular functions. The discovery of this surprisingly large family of calpain-like proteins in lower eukaryotes that combines novel and conserved sequence modules contributes to our understanding of the evolution of this abundant protein family. |
| first_indexed | 2024-03-06T23:25:11Z |
| format | Journal article |
| id | oxford-uuid:6a20e6ff-7bbb-48cf-8f31-01dd1eb3f89d |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:25:11Z |
| publishDate | 2005 |
| record_format | dspace |
| spelling | oxford-uuid:6a20e6ff-7bbb-48cf-8f31-01dd1eb3f89d2022-03-26T18:55:22ZEvolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6a20e6ff-7bbb-48cf-8f31-01dd1eb3f89dEnglishSymplectic Elements at Oxford2005Ersfeld, KBarraclough, HGull, KEmploying whole-genome analysis we have characterized a large family of genes coding for calpain-related proteins in three kinetoplastid parasites. We have defined a total of 18 calpain-like sequences in Trypanosoma brucei, 27 in Leishmania major, and 24 in Trypanosoma cruzi. Sequence characterization revealed a well-conserved protease domain in most proteins, although residues critical for catalytic activity were frequently altered. Many of the proteins contain a novel N-terminal sequence motif unique to kinetoplastids. Furthermore, 24 of the sequences contain N-terminal fatty acid acylation motifs indicating association of these proteins with intracellular membranes. This extended family of proteins also includes a group of sequences that completely lack a protease domain but is specifically related to other kinetoplastid calpain-related proteins by a highly conserved N-terminal domain and by genomic organization. All sequences lack the C-terminal calmodulin-related calcium-binding domain typical of most mammalian calpains. Our analysis emphasizes the highly modular structure of calpains and calpain-like proteins, suggesting that they are involved in diverse cellular functions. The discovery of this surprisingly large family of calpain-like proteins in lower eukaryotes that combines novel and conserved sequence modules contributes to our understanding of the evolution of this abundant protein family. |
| spellingShingle | Ersfeld, K Barraclough, H Gull, K Evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites. |
| title | Evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites. |
| title_full | Evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites. |
| title_fullStr | Evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites. |
| title_full_unstemmed | Evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites. |
| title_short | Evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites. |
| title_sort | evolutionary relationships and protein domain architecture in an expanded calpain superfamily in kinetoplastid parasites |
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