Selenocysteine incorporation in Kinetoplastid: Selenophosphate synthetase (SELD) from Leishmania major and Trypanosoma brucei

Sculaccio, Susana Andréa; Rodrigues, Érico; Cordeiro, Artur T.; Magalhães, Alviclér; Braga, Antônio L.; Alberto, Eduardo E.; Thiemann, Otávio Henrique

doi:10.1016/j.molbiopara.2008.08.009

Cited by 24 publications

(24 citation statements)

References 28 publications

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“…Moreover, in silico screens by several groups have identified Tb-tRNA Sec , Tb-SerRS, Tb-PSTK, TbSepSecS, Tb-SPS2, and Tb-EFSec, the trypanosomal orthologues of essentially all major components of the Sec-inserting system (16). However, of these only Tb-SerRS, Tb-tRNA Sec (16)(17)(18), and Tb-SPS2 (19) have been subject to preliminary experimental analyses.…”

Section: T Brucei Components Involved In Selenoprotein Formationmentioning

confidence: 99%

“…Mammalian SPS2, which itself is a selenoprotein, is essential for selenoprotein synthesis in vivo (8). Tb-SPS2 an SPS2 orthologue capable of complementing SelA-deficient Escherichia coli has been identified in trypanosomatids (19). Like the E. coli orthologue, but in contrast to its mammalian counterpart, Tb-SPS2 is not a selenoprotein.…”

Section: T Brucei Components Involved In Selenoprotein Formationmentioning

confidence: 99%

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The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes

Aeby

Palioura²,

Pusnik

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Section: T Brucei Components Involved In Selenoprotein Formationmentioning

confidence: 99%

Section: T Brucei Components Involved In Selenoprotein Formationmentioning

confidence: 99%

The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes

Aeby

Palioura²,

Pusnik

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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“…Cloning (6) Functional Complementation Assay-The functional complementation experiments were conducted according to Sculaccio et al (16) for N-terminally truncated SPS. Briefly, the E. coli strain WL400 (DE3), which lacks the functional selD gene (7), was transformed with the full-length E. coli SPS sequence and the SPS construct lacking the N-terminal 11 residues (⌬11-SPS).…”

Section: Methodsmentioning

confidence: 99%

“…Briefly, the E. coli strain WL400 (DE3), which lacks the functional selD gene (7), was transformed with the full-length E. coli SPS sequence and the SPS construct lacking the N-terminal 11 residues (⌬11-SPS). These cells were tested for the presence of an active selenoprotein formate dehydrogenase H (FDH H) using the benzyl viologen assay under anaerobic conditions (16). Similarly, the SelA and N-terminally truncated SelA complementation experiments were performed using this methodology using the E. coli strain JS1 (DE3), which lacks the functional selA gene, under the same anaerobic conditions (16) for 48 h in 30°C.…”

Section: Methodsmentioning

confidence: 99%

Formation of a Ternary Complex for Selenocysteine Biosynthesis in Bacteria

Silva

Serrão

Manzine

et al. 2015

Journal of Biological Chemistry

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Background: Selenoprotein biosynthesis requires the interaction of tRNA Sec and specific enzymes that drive the synthesis of selenocysteine. Results: Formation of a molecular complex of selenophosphate synthetase, selenocysteine synthase, and tRNA Sec was identified and characterized. Conclusion:The ternary complex formation is necessary for selenoprotein synthesis.Significance: Our findings demonstrate the formation of a ternary complex and provide a possible scenario for selenium metabolism in bacteria.

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“…The insertion of selenium into Sec-dependent enzymes requires the formation of a highly reactive reduced selenium donor compound monoselenophosphate. Monoselenophosphate synthesis is catalyzed by SPS in a 1:1 ratio from selenide and ATP [5,[15][16][17].…”

Section: Specific Characteristics Of Kinetoplas-tid Selenocysteine Bimentioning

confidence: 99%

Biological Implications of Selenium and its Role in Trypanosomiasis Treatment

Silva¹,

Silva²,

Thiemann³

2014

CMC

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Selenium (Se) is an essential trace element for several organisms and is present in proteins as selenocysteine (Sec or U), an amino acid that is chemically distinct from serine and cysteine by a single atom (Se instead of O or S, respectively). Sec is incorporated into selenoproteins at an in-frame UGA codon specified by an mRNA stem-loop structure called the selenocysteine incorporating sequence (SECIS) presented in selenoprotein mRNA and specific selenocysteine synthesis and incorporation machinery. Selenoproteins are presented in all domains but are not found in all organisms. Although several functions have been attributed to this class, the majority of the proteins are involved in oxidative stress defense. Here, we discuss the kinetoplastid selenocysteine pathway and how selenium supplementation is able to alter the infection course of trypanosomatids in detail. These organisms possess the canonical elements required for selenoprotein production such as phosphoseryl tRNA kinase (PSTK), selenocysteine synthase (SepSecS), selenophosphase synthase (SelD or SPS), and elongation factor EFSec (SelB), whereas other important factors presented in mammal cells, such as SECIS binding protein 2 (SBP) and SecP 43, are absent. The selenoproteome of trypanosomatids is small, as is the selenoproteome of others parasites, which is in contrast to the large number of selenoproteins found in bacteria, aquatic organisms and higher eukaryotes. Trypanosoma and Leishmania are sensitive to auranofin, a potent selenoprotein inhibitor; however, the probable drug mechanism is not related to selenoproteins in kinetoplastids. Selenium supplementation decreases the parasitemia of various Trypanosome infections and reduces important parameters associated with diseases such as anemia and parasite-induced organ damage. New experiments are necessary to determine how selenium acts, but evidence suggests that immune response modulation and increased host defense against oxidative stress contribute to control of the parasite infection.

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Selenocysteine incorporation in Kinetoplastid: Selenophosphate synthetase (SELD) from Leishmania major and Trypanosoma brucei

Cited by 24 publications

References 28 publications

The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes

The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes

Formation of a Ternary Complex for Selenocysteine Biosynthesis in Bacteria

Biological Implications of Selenium and its Role in Trypanosomiasis Treatment

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