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Tytuł pozycji:

The Leishmania donovani SENP Protease Is Required for SUMO Processing but Not for Viability.

Tytuł:
The Leishmania donovani SENP Protease Is Required for SUMO Processing but Not for Viability.
Autorzy:
Bea A; Leishmaniasis Group, Bernhard Nocht Institute for Tropical Medicine, D-20359 Hamburg, Germany.
Kröber-Boncardo C; Leishmaniasis Group, Bernhard Nocht Institute for Tropical Medicine, D-20359 Hamburg, Germany.
Sandhu M; Leishmaniasis Group, Bernhard Nocht Institute for Tropical Medicine, D-20359 Hamburg, Germany.; Boehringer Ingelheim RCV, A-1121 Vienna, Austria.
Brinker C; Leishmaniasis Group, Bernhard Nocht Institute for Tropical Medicine, D-20359 Hamburg, Germany.
Clos J; Leishmaniasis Group, Bernhard Nocht Institute for Tropical Medicine, D-20359 Hamburg, Germany.
Źródło:
Genes [Genes (Basel)] 2020 Oct 14; Vol. 11 (10). Date of Electronic Publication: 2020 Oct 14.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Original Publication: Basel : MDPI
MeSH Terms:
Protein Processing, Post-Translational*
Sumoylation*
Cysteine Endopeptidases/*metabolism
Leishmania donovani/*metabolism
Leishmaniasis/*parasitology
Macrophages/*cytology
Small Ubiquitin-Related Modifier Proteins/*metabolism
Animals ; Cells, Cultured ; Cysteine Endopeptidases/genetics ; Leishmania donovani/genetics ; Leishmaniasis/genetics ; Leishmaniasis/metabolism ; Macrophages/metabolism ; Macrophages/parasitology ; Mice ; Small Ubiquitin-Related Modifier Proteins/genetics ; Substrate Specificity
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Contributed Indexing:
Keywords: CRISPR; Leishmania; SENP; SUMO; Ulp2; protease
Substance Nomenclature:
0 (Small Ubiquitin-Related Modifier Proteins)
EC 3.4.22.- (Cysteine Endopeptidases)
Entry Date(s):
Date Created: 20201017 Date Completed: 20210715 Latest Revision: 20210715
Update Code:
20240105
PubMed Central ID:
PMC7602377
DOI:
10.3390/genes11101198
PMID:
33066659
Czasopismo naukowe
The protozoan parasite Leishmania donovani is part of an early eukaryotic branch and depends on post-transcriptional mechanisms for gene expression regulation. This includes post-transcriptional protein modifications, such as protein phosphorylation. The presence of genes for protein SUMOylation, i.e., the covalent attachment of small ubiquitin-like modifier (SUMO) polypeptides, in the Leishmania genomes prompted us to investigate the importance of the sentrin-specific protease (SENP) and its putative client, SUMO, for the vitality and infectivity of Leishmania donovani . While SENP null mutants are viable with reduced vitality, viable SUMO null mutant lines could not be obtained. SUMO C-terminal processing is disrupted in SENP null mutants, preventing SUMO from covalent attachment to proteins and nuclear translocation. Infectivity in vitro is not affected by the loss of SENP-dependent SUMO processing. We conclude that SENP is required for SUMO processing, but that functions of unprocessed SUMO are critical for Leishmania viability.
Competing Interests: The authors declare no conflict of interest.

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