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Comprehensive sub-mitochondrial protein map of the parasitic protist Trypanosoma brucei defines critical features of organellar biology
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SYSNO ASEP 0576576 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Comprehensive sub-mitochondrial protein map of the parasitic protist Trypanosoma brucei defines critical features of organellar biology Author(s) Pyrih, Jan (BC-A) ORCID
Hammond, Michael John (BC-A) SAI, ORCID
Alves, A. (GB)
Dean, S. (GB)
Sunter, J.D. (GB)
Wheeler, R. J. (GB)
Gull, K. (GB)
Lukeš, Julius (BC-A) RID, ORCIDNumber of authors 8 Article number 113083 Source Title Cell Reports. - : Cell Press - ISSN 2211-1247
Roč. 42, č. 9 (2023)Number of pages 19 s. Publication form Online - E Language eng - English Country US - United States Keywords METABOLIC ; organellar ; Trypanosoma brucei Subject RIV EE - Microbiology, Virology OECD category Microbiology R&D Projects GA21-09283S GA ČR - Czech Science Foundation (CSF) EF16_019/0000759 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support BC-A - RVO:60077344 UT WOS 001073362600001 EID SCOPUS 85169920202 DOI 10.1016/j.celrep.2023.113083 Annotation We have generated a high-confidence mitochondrial proteome (MitoTag) of the Trypanosoma brucei procy-clic stage containing 1,239 proteins. For 337 of these, a mitochondrial localization had not been described before. We use the TrypTag dataset as a foundation and take advantage of the properties of the fluorescent protein tag that causes aberrant but fortuitous accumulation of tagged matrix and inner membrane proteins near the kinetoplast (mitochondrial DNA). Combined with transmembrane domain predictions, this charac-teristic allowed categorization of 1,053 proteins into mitochondrial sub-compartments, the detection of unique matrix-localized fucose and methionine synthesis, and the identification of new kinetoplast proteins, which showed kinetoplast-linked pyrimidine synthesis. Moreover, disruption of targeting signals by tagging allowed mapping of the mode of protein targeting to these sub-compartments, identifying a set of C-tail anchored outer mitochondrial membrane proteins and mitochondrial carriers likely employing multiple target peptides. This dataset represents a comprehensive, updated mapping of the mitochondrion. Workplace Biology Centre (since 2006) Contact Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Year of Publishing 2024 Electronic address https://www.sciencedirect.com/science/article/pii/S221112472301094X?via%3Dihub
Number of the records: 1