Počet záznamů: 1
Functions and cellular localization of cysteine desulfurase and selenocysteine lyase in Trypanosoma brucei
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SYSNO ASEP 0342953 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Functions and cellular localization of cysteine desulfurase and selenocysteine lyase in Trypanosoma brucei Tvůrce(i) Poliak, Pavel (BC-A)
Van Hoewyk, D. (US)
Oborník, Miroslav (BC-A) RID, ORCID
Zíková, Alena (BC-A) RID, ORCID
Stuart, K. D. (US)
Tachezy, J. (CZ)
Pilon, M. (US)
Lukeš, Julius (BC-A) RID, ORCIDZdroj.dok. FEBS Journal - ISSN 1742-464X
Roč. 277, č. 2 (2010), s. 383-393Poč.str. 11 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova Fe–S cluster ; mitochondrion ; RNAi ; selenoprotein ; Trypanosoma Vědní obor RIV EB - Genetika a molekulární biologie CEP GA204/09/1667 GA ČR - Grantová agentura ČR CEZ AV0Z60220518 - PAU-O, BC-A (2005-2011) UT WOS 000273396000013 DOI 10.1111/j.1742-4658.2009.07489.x Anotace It was shown previously that the Nfs-like protein called Nfs from the parasitic protist Trypanosoma brucei is a genuine CysD. A second Nfs-like protein is encoded in the nuclear genome of T. brucei. We called this protein selenocysteine lyase (SCL) because phylogenetic analysis reveals that it is monophyletic with known eukaryotic selenocysteine lyases. The Nfs protein is located in the mitochondrion, whereas the SCL protein seems to be present in the nucleus and cytoplasm. Unexpectedly, downregulation of either Nfs or SCL protein leads to a dramatic decrease in both CysD and selenocysteine lyase activities concurrently in the mitochondrion and the cytosolic fractions. Because loss of Nfs causes a growth phenotype but loss of SCL does not, we propose that Nfs can fully complement SCL, whereas SCL can only partially replace Nfs under our growth conditions. Pracoviště Biologické centrum (od r. 2006) Kontakt Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Rok sběru 2011
Počet záznamů: 1