Dihydrouridine synthase (Dus) | |||||||||
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Identifiers | |||||||||
Symbol | Dus | ||||||||
Pfam | PF01207 | ||||||||
Pfam clan | CL0036 | ||||||||
InterPro | IPR001269 | ||||||||
PROSITE | PDOC00874 | ||||||||
SCOP2 | 1vhn / SCOPe / SUPFAM | ||||||||
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In molecular biology, tRNA-dihydrouridine synthase is a family of enzymes which catalyse the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae (Baker's yeast) acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. [1] [2] Some family members may be targeted to the mitochondria and even have a role in mitochondria. [2]
Saccharomyces cerevisiae is a species of yeast. The species has been instrumental in winemaking, baking, and brewing since ancient times. It is believed to have been originally isolated from the skin of grapes. It is one of the most intensively studied eukaryotic model organisms in molecular and cell biology, much like Escherichia coli as the model bacterium. It is the microorganism which causes many common types of fermentation. S. cerevisiae cells are round to ovoid, 5–10 μm in diameter. It reproduces by budding.
Sphingolipids are a class of lipids containing a backbone of sphingoid bases, which are a set of aliphatic amino alcohols that includes sphingosine. They were discovered in brain extracts in the 1870s and were named after the mythological sphinx because of their enigmatic nature. These compounds play important roles in signal transduction and cell recognition. Sphingolipidoses, or disorders of sphingolipid metabolism, have particular impact on neural tissue. A sphingolipid with a terminal hydroxyl group is a ceramide. Other common groups bonded to the terminal oxygen atom include phosphocholine, yielding a sphingomyelin, and various sugar monomers or dimers, yielding cerebrosides and globosides, respectively. Cerebrosides and globosides are collectively known as glycosphingolipids.
RNA editing is a molecular process through which some cells can make discrete changes to specific nucleotide sequences within an RNA molecule after it has been generated by RNA polymerase. It occurs in all living organisms and is one of the most evolutionarily conserved properties of RNAs. RNA editing may include the insertion, deletion, and base substitution of nucleotides within the RNA molecule. RNA editing is relatively rare, with common forms of RNA processing not usually considered as editing. It can affect the activity, localization as well as stability of RNAs, and has been linked with human diseases.
Pseudouridine is an isomer of the nucleoside uridine in which the uracil is attached via a carbon-carbon instead of a nitrogen-carbon glycosidic bond.
The mating-type locus is a specialized region in the genomes of some yeast and other fungi, usually organized into heterochromatin and possessing unique histone methylation patterns. The genes in this region regulate the mating type of the organism and therefore determine key events in its life cycle, such as whether it will reproduce sexually or asexually. In fission yeast such as S. pombe, the formation and maintenance of the heterochromatin organization is regulated by RNA-induced transcriptional silencing, a form of RNA interference responsible for genomic maintenance in many organisms. Mating type regions have also been well studied in budding yeast S. cerevisiae and in the fungus Neurospora crassa.
In molecular biology, Small nucleolar RNA R66 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA.
In molecular biology, the snoRNA snR48 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA.
In molecular biology, snoRNA snR71 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA snR71 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. snoRNA snR71 was initially discovered using a computational screen of the Saccharomyces cerevisiae genome.
TRAMP complex is a multiprotein, heterotrimeric complex having distributive polyadenylation activity and identifies wide varieties of RNAs produced by polymerases. It was originally discovered in Saccharomycescerevisiae by LaCava et al., Vanacova et al. and Wyers et al. in 2005.
In enzymology, a 2'-phosphotransferase (EC 2.7.1.160) is an enzyme that catalyzes the chemical reaction
In enzymology, a tRNA nucleotidyltransferase is an enzyme that catalyzes the chemical reaction
GCN2 is a serine/threonine-protein kinase that senses amino acid deficiency through binding to uncharged transfer RNA (tRNA). It plays a key role in modulating amino acid metabolism as a response to nutrient deprivation.
TRNA-dihydrouridine16/17 synthase (NAD(P)+) (EC 1.3.1.88, Dus1p, tRNA-dihydrouridine synthase 1) is an enzyme with systematic name tRNA-5,6-dihydrouracil16/17:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction
TRNA-dihydrouridine47 synthase (NAD(P)+) (EC 1.3.1.89, Dus3p, tRNA-dihydrouridine synthase 3) is an enzyme with systematic name tRNA-5,6-dihydrouracil47:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction
TRNA-dihydrouridine20a/20b synthase (NAD(P)+) (EC 1.3.1.90, Dus4p) is an enzyme with systematic name tRNA-5,6-dihydrouracil20a/20b:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction
TRNA-dihydrouridine20 synthase (NAD(P)+) (EC 1.3.1.91, Dus2p, tRNA-dihydrouridine synthase 2) is an enzyme with systematic name tRNA-5,6-dihydrouracil20:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction
TRNA (guanine9-N1)-methyltransferase (EC 2.1.1.221, Trm10p, tRNA(m1G9/m1A9)-methyltransferase, tRNA(m1G9/m1A9)MTase, tRNA (guanine-N(1)-)-methyltransferase, tRNA m1G9-methyltransferase, tRNA m1G9 MTase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine9-N1)-methyltransferase. This enzyme catalyses the following chemical reaction
TRNA:m4X modification enzyme is an enzyme with systematic name S-adenosyl-L-methionine:tRNAPro/His/Gly(GCC) (cytidine/adenosine4-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction
tRNA(His) guanylyltransferase is an enzyme with systematic name p-tRNA(His):GTP guanylyltransferase (ATP-hydrolysing). This enzyme catalyses the following chemical reaction
tRNA pseudouridine13 synthase is an enzyme with systematic name tRNA-uridine13 uracil mutase. This enzyme catalyses the following chemical reaction