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Statements

Subject Item
n2:RIV%2F00064165%3A_____%2F13%3A10192000%21RIV14-MZ0-00064165
rdf:type
skos:Concept n6:Vysledek
rdfs:seeAlso
http://dx.doi.org/10.1016/j.bbapap.2013.09.020
dcterms:description
O-Acetylserine(thiol)lyases (OAS-TLs) play a pivotal role in a sulfur assimilation pathway incorporating sulfide into amino acids in microorganisms and plants, however, these enzymes have not been found in the animal kingdom. Interestingly, the genome of the roundworm Caenorhabditis elegans contains three expressed genes predicted to encode OAS-TL orthologs (cysl-1-cysl-3), and a related pseudogene (cysl-4); these genes play different roles in resistance to hypoxia, hydrogen sulfide and cyanide. To get an insight into the underlying molecular mechanisms we purified the three recombinant worm OAS-TL proteins, and we determined their enzymatic activities, substrate binding affinities, quaternary structures and the conformations of their active site shapes. We show that the nematode OAS-TL orthologs can bind O-acetylserine and catalyze the canonical reaction although this ligand may more likely serve as a competitive inhibitor to natural substrates instead of being a substrate for sulfur assimilation. In addition, we propose that S-sulfocysteine may be a novel endogenous substrate for these proteins. However, we observed that the three OAS-TL proteins are conformationally different and exhibit distinct substrate specificity. Based on the available evidences we propose the following model: CYSL-1 interacts with EGL-9 and activates HIF-1 that upregulates expression of genes detoxifying sulfide and cyanide, the CYSL-2 acts as a cyanoalanine synthase in the cyanide detoxification pathway and simultaneously produces hydrogen sulfide, while the role of CYSL-3 remains unclear although it exhibits sulfhydrylase activity in vitro. All these data indicate that C. elegans OAS-TL paralogs have distinct cellular functions and may play different roles in maintaining hydrogen sulfide homeostasis. O-Acetylserine(thiol)lyases (OAS-TLs) play a pivotal role in a sulfur assimilation pathway incorporating sulfide into amino acids in microorganisms and plants, however, these enzymes have not been found in the animal kingdom. Interestingly, the genome of the roundworm Caenorhabditis elegans contains three expressed genes predicted to encode OAS-TL orthologs (cysl-1-cysl-3), and a related pseudogene (cysl-4); these genes play different roles in resistance to hypoxia, hydrogen sulfide and cyanide. To get an insight into the underlying molecular mechanisms we purified the three recombinant worm OAS-TL proteins, and we determined their enzymatic activities, substrate binding affinities, quaternary structures and the conformations of their active site shapes. We show that the nematode OAS-TL orthologs can bind O-acetylserine and catalyze the canonical reaction although this ligand may more likely serve as a competitive inhibitor to natural substrates instead of being a substrate for sulfur assimilation. In addition, we propose that S-sulfocysteine may be a novel endogenous substrate for these proteins. However, we observed that the three OAS-TL proteins are conformationally different and exhibit distinct substrate specificity. Based on the available evidences we propose the following model: CYSL-1 interacts with EGL-9 and activates HIF-1 that upregulates expression of genes detoxifying sulfide and cyanide, the CYSL-2 acts as a cyanoalanine synthase in the cyanide detoxification pathway and simultaneously produces hydrogen sulfide, while the role of CYSL-3 remains unclear although it exhibits sulfhydrylase activity in vitro. All these data indicate that C. elegans OAS-TL paralogs have distinct cellular functions and may play different roles in maintaining hydrogen sulfide homeostasis.
dcterms:title
Biochemical properties of nematode O-acetylserine(thiol)lyase paralogs imply their distinct roles in hydrogen sulfide homeostasis Biochemical properties of nematode O-acetylserine(thiol)lyase paralogs imply their distinct roles in hydrogen sulfide homeostasis
skos:prefLabel
Biochemical properties of nematode O-acetylserine(thiol)lyase paralogs imply their distinct roles in hydrogen sulfide homeostasis Biochemical properties of nematode O-acetylserine(thiol)lyase paralogs imply their distinct roles in hydrogen sulfide homeostasis
skos:notation
RIV/00064165:_____/13:10192000!RIV14-MZ0-00064165
n6:predkladatel
n7:ico%3A00064165
n4:aktivita
n15:I n15:Z
n4:aktivity
I, Z(MSM6046137305)
n4:cisloPeriodika
12
n4:dodaniDat
n17:2014
n4:domaciTvurceVysledku
n10:3950131 n10:9185283
n4:druhVysledku
n13:J
n4:duvernostUdaju
n20:S
n4:entitaPredkladatele
n16:predkladatel
n4:idSjednocenehoVysledku
63380
n4:idVysledku
RIV/00064165:_____/13:10192000
n4:jazykVysledku
n12:eng
n4:klicovaSlova
C. elegans; Cysteine synthase; O-Acetylserine sulfhydrylase; S-Sulfocysteine; Cyanide; Hydrogen sulfide
n4:klicoveSlovo
n5:Hydrogen%20sulfide n5:Cyanide n5:O-Acetylserine%20sulfhydrylase n5:C.%20elegans n5:S-Sulfocysteine n5:Cysteine%20synthase
n4:kodStatuVydavatele
NL - Nizozemsko
n4:kontrolniKodProRIV
[C756DDE61E44]
n4:nazevZdroje
Biochimica et Biophysica Acta - Proteins and Proteomics
n4:obor
n19:CE
n4:pocetDomacichTvurcuVysledku
2
n4:pocetTvurcuVysledku
5
n4:rokUplatneniVysledku
n17:2013
n4:svazekPeriodika
1834
n4:tvurceVysledku
Hnízda, Aleš Šerá, Leona Kožich, Viktor Krijt, Jakub Vozdek, Roman
n4:wos
000329418300027
n4:zamer
n14:MSM6046137305
s:issn
1570-9639
s:numberOfPages
11
n8:doi
10.1016/j.bbapap.2013.09.020