Queuosine

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Queuosine
Queuosine - Queuosin.svg
Names
IUPAC name
7-({[(1S,4S,5R)-4,5-Dihydroxycyclopent-2-en-1-yl]amino}methyl)-7-carbaguanosine
Systematic IUPAC name
2-Amino-5-({[(1S,4S,5R)-4,5-dihydroxycyclopent-2-en-1-yl]amino}methyl)-7-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Identifiers
3D model (JSmol)
ChemSpider
PubChem CID
  • InChI=1S/C17H23N5O7/c18-17-20-14-10(15(28)21-17)6(3-19-7-1-2-8(24)11(7)25)4-22(14)16-13(27)12(26)9(5-23)29-16/h1-2,4,7-9,11-13,16,19,23-27H,3,5H2,(H3,18,20,21,28)/t7-,8-,9+,11+,12+,13+,16+/m0/s1 X mark.svgN
    Key: QQXQGKSPIMGUIZ-AEZJAUAXSA-N X mark.svgN
  • InChI=1/C17H23N5O7/c18-17-20-14-10(15(28)21-17)6(3-19-7-1-2-8(24)11(7)25)4-22(14)16-13(27)12(26)9(5-23)29-16/h1-2,4,7-9,11-13,16,19,23-27H,3,5H2,(H3,18,20,21,28)/t7-,8-,9+,11+,12+,13+,16+/m0/s1
    Key: QQXQGKSPIMGUIZ-AEZJAUAXBO
  • C1=C[C@@H]([C@@H]([C@H]1NCC2=CN(C3=C2C(=O)N=C(N3)N)[C@H]4[C@@H]([C@@H]([C@H](O4)CO)O)O)O)O
Properties
C17H23N5O7
Molar mass 409.399 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
X mark.svgN  verify  (what is  Yes check.svgYX mark.svgN ?)

Queuosine is a modified nucleoside that is present in certain tRNAs in bacteria and eukaryotes. [1] [2] It contains the nucleobase queuine. Originally identified in E. coli , queuosine was found to occupy the first anticodon position of tRNAs for histidine, aspartic acid, asparagine and tyrosine. [3] The first anticodon position pairs with the third "wobble" position in codons, and queuosine improves accuracy of translation compared to guanosine. [4] [5] [6] Synthesis of queuosine begins with GTP. In bacteria, three structurally unrelated classes of riboswitch are known to regulate genes that are involved in the synthesis or transport of pre-queuosine1, a precursor to queuosine: PreQ1-I riboswitches, PreQ1-II riboswitches and PreQ1-III riboswitches.

Queuosine biosynthesis genes have also been found on phage genomes and may be involved in protection from genome degradation by the host. [7] [8]

Related Research Articles

<span class="mw-page-title-main">RNA</span> Family of large biological molecules

Ribonucleic acid (RNA) is a polymeric molecule that is essential for most biological functions, either by performing the function itself or by forming a template for the production of proteins. RNA and deoxyribonucleic acid (DNA) are nucleic acids. The nucleic acids constitute one of the four major macromolecules essential for all known forms of life. RNA is assembled as a chain of nucleotides. Cellular organisms use messenger RNA (mRNA) to convey genetic information that directs synthesis of specific proteins. Many viruses encode their genetic information using an RNA genome.

<span class="mw-page-title-main">Stop codon</span> Codon that marks the end of a protein-coding sequence

In molecular biology, a stop codon is a codon that signals the termination of the translation process of the current protein. Most codons in messenger RNA correspond to the addition of an amino acid to a growing polypeptide chain, which may ultimately become a protein; stop codons signal the termination of this process by binding release factors, which cause the ribosomal subunits to disassociate, releasing the amino acid chain.

<span class="mw-page-title-main">Translation (biology)</span> Cellular process of protein synthesis

In biology, translation is the process in living cells in which proteins are produced using RNA molecules as templates. The generated protein is a sequence of amino acids. This sequence is determined by the sequence of nucleotides in the RNA. The nucleotides are considered three at a time. Each such triple results in addition of one specific amino acid to the protein being generated. The matching from nucleotide triple to amino acid is called the genetic code. The translation is performed by a large complex of functional RNA and proteins called ribosomes. The entire process is called gene expression.

<span class="mw-page-title-main">Transfer RNA</span> RNA that facilitates the addition of amino acids to a new protein

Transfer RNA is an adaptor molecule composed of RNA, typically 76 to 90 nucleotides in length. In a cell, it provides the physical link between the genetic code in messenger RNA (mRNA) and the amino acid sequence of proteins, carrying the correct sequence of amino acids to be combined by the protein-synthesizing machinery, the ribosome. Each three-nucleotide codon in mRNA is complemented by a three-nucleotide anticodon in tRNA. As such, tRNAs are a necessary component of translation, the biological synthesis of new proteins in accordance with the genetic code.

<span class="mw-page-title-main">Wobble base pair</span> RNA base pair that does not follow Watson-Crick base pair rules

A wobble base pair is a pairing between two nucleotides in RNA molecules that does not follow Watson-Crick base pair rules. The four main wobble base pairs are guanine-uracil (G-U), hypoxanthine-uracil (I-U), hypoxanthine-adenine (I-A), and hypoxanthine-cytosine (I-C). In order to maintain consistency of nucleic acid nomenclature, "I" is used for hypoxanthine because hypoxanthine is the nucleobase of inosine; nomenclature otherwise follows the names of nucleobases and their corresponding nucleosides. The thermodynamic stability of a wobble base pair is comparable to that of a Watson-Crick base pair. Wobble base pairs are fundamental in RNA secondary structure and are critical for the proper translation of the genetic code.

The Shine–Dalgarno (SD) sequence is a ribosomal binding site in bacterial and archaeal messenger RNA, generally located around 8 bases upstream of the start codon AUG. The RNA sequence helps recruit the ribosome to the messenger RNA (mRNA) to initiate protein synthesis by aligning the ribosome with the start codon. Once recruited, tRNA may add amino acids in sequence as dictated by the codons, moving downstream from the translational start site.

<span class="mw-page-title-main">RNA editing</span> Molecular process

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.

<span class="mw-page-title-main">Pseudouridine</span> Chemical compound

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.

<span class="mw-page-title-main">Start codon</span> First codon of a messenger RNA translated by a ribosome

The start codon is the first codon of a messenger RNA (mRNA) transcript translated by a ribosome. The start codon always codes for methionine in eukaryotes and archaea and a N-formylmethionine (fMet) in bacteria, mitochondria and plastids.

<span class="mw-page-title-main">EF-Tu</span> Prokaryotic elongation factor

EF-Tu is a prokaryotic elongation factor responsible for catalyzing the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome. It is a G-protein, and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome. As a reflection of its crucial role in translation, EF-Tu is one of the most abundant and highly conserved proteins in prokaryotes. It is found in eukaryotic mitochondria as TUFM.

<span class="mw-page-title-main">Queuine</span> Chemical compound

Queuine (Q) is a hypermodified nucleobase found in the first position of the anticodon of tRNAs specific for Asn, Asp, His, and Tyr, in most eukaryotes and prokaryotes. Because it is utilized by all eukaryotes but produced exclusively by bacteria, it is a putative vitamin.

A bacterial initiation factor (IF) is a protein that stabilizes the initiation complex for polypeptide translation.

<span class="mw-page-title-main">PreQ1 riboswitch</span>

The PreQ1-I riboswitch is a cis-acting element identified in bacteria which regulates expression of genes involved in biosynthesis of the nucleoside queuosine (Q) from GTP. PreQ1 (pre-queuosine1) is an intermediate in the queuosine pathway, and preQ1 riboswitch, as a type of riboswitch, is an RNA element that binds preQ1. The preQ1 riboswitch is distinguished by its unusually small aptamer, compared to other riboswitches. Its atomic-resolution three-dimensional structure has been determined, with the PDB ID 2L1V.

In enzymology, a preQ1 synthase (EC 1.7.1.13) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">TRMU</span> Protein-coding gene in the species Homo sapiens

Mitochondrial tRNA-specific 2-thiouridylase 1 is an enzyme that in humans is encoded by the TRMU gene.

<span class="mw-page-title-main">PreQ1-II riboswitch</span> Class of riboswitches

PreQ1-II riboswitches form a class of riboswitches that specifically bind pre-queuosine1 (PreQ1), a precursor of the modified nucleoside queuosine. They are found in certain species of Streptococcus and Lactococcus, and were originally identified as a conserved RNA secondary structure called the "COG4708 motif". All known members of this riboswitch class appear to control members of COG4708 genes. These genes are predicted to encode membrane-bound proteins and have been proposed to be a transporter of preQ1, or a related metabolite, based on their association with preQ1-binding riboswitches. PreQ1-II riboswitches have no apparent similarities in sequence or structure to preQ1-I riboswitches, a previously discovered class of preQ1-binding riboswitches. PreQ1 thus joins S-adenosylmethionine as the second metabolite to be found that is the ligand of more than one riboswitch class.

Translational regulation refers to the control of the levels of protein synthesized from its mRNA. This regulation is vastly important to the cellular response to stressors, growth cues, and differentiation. In comparison to transcriptional regulation, it results in much more immediate cellular adjustment through direct regulation of protein concentration. The corresponding mechanisms are primarily targeted on the control of ribosome recruitment on the initiation codon, but can also involve modulation of peptide elongation, termination of protein synthesis, or ribosome biogenesis. While these general concepts are widely conserved, some of the finer details in this sort of regulation have been proven to differ between prokaryotic and eukaryotic organisms.

<span class="mw-page-title-main">Agmatidine</span> Chemical compound

Agmatidine (2-agmatinylcytidine, symbol C+ or agm2C) is a modified cytidine present in the wobble position of the anticodon of several archaeal AUA decoding tRNAs. Agmatidine is essential for correct decoding of the AUA codon in many archaea and is required for aminoacylation of tRNAIle2 with isoleucine.

<span class="mw-page-title-main">Wybutosine</span> Chemical compound

In biochemistry, wybutosine (yW) is a heavily modified nucleoside of phenylalanine transfer RNA that stabilizes interactions between the codons and anti-codons during protein synthesis. Ensuring accurate synthesis of protein is essential in maintaining health as defects in tRNA modifications are able to cause disease. In eukaryotic organisms, it is found only in position 37, 3'-adjacent to the anticodon, of phenylalanine tRNA. Wybutosine enables correct translation through the stabilization of the codon-anticodon base pairing during the decoding process.

<span class="mw-page-title-main">PreQ1-III riboswitch</span>

PreQ1-III riboswitches are a class of riboswitches that bind pre-queuosine1 (PreQ1), a precursor to the modified nucleoside queuosine. PreQ1-III riboswitches are the third class of riboswitches to be discovered that sense this ligand, and are structurally distinct from preQ1-I and preQ1-II riboswitches. Most sequenced examples of preQ1-III riboswitches are obtained from uncultivated metagenome samples, but the few examples in cultivated organisms are present in strains that are known to or suspected to be Faecalibacterium prausnitzii, a species of Gram-positive Clostridia. Known examples of preQ1-III riboswitches are found upstream of queT genes, which are expected to encode transporters of a queuosine derivative. The other two known classes of preQ1 riboswitches are also commonly found upstream of queT genes.

References

  1. Iwata-Reuyl D (February 2003). "Biosynthesis of the 7-deazaguanosine hypermodified nucleosides of transfer RNA". Bioorganic Chemistry. 31 (1): 24–43. doi:10.1016/S0045-2068(02)00513-8. PMID   12697167.
  2. Morris RC, Elliott MS (2001). "Queuosine modification of tRNA: a case for convergent evolution". Molecular Genetics and Metabolism. 74 (1–2): 147–159. doi:10.1006/mgme.2001.3216. PMID   11592812.
  3. Harada F, Nishimura S (January 1972). "Possible anticodon sequences of tRNA His , tRNA Asm , and tRNA Asp from Escherichia coli B. Universal presence of nucleoside Q in the first postion of the anticondons of these transfer ribonucleic acids". Biochemistry. 11 (2): 301–308. doi:10.1021/bi00752a024. PMID   4550561.
  4. Bienz M, Kubli E (November 1981). "Wild-type tRNATyrG reads the TMV RNA stop codon, but Q base-modified tRNATyrQ does not". Nature. 294 (5837): 188–190. Bibcode:1981Natur.294..188B. doi:10.1038/294188a0. PMID   29451243. S2CID   204999725.
  5. Meier F, Suter B, Grosjean H, Keith G, Kubli E (March 1985). "Queuosine modification of the wobble base in tRNAHis influences 'in vivo' decoding properties". The EMBO Journal. 4 (3): 823–827. doi:10.1002/j.1460-2075.1985.tb03704.x. PMC   554263 . PMID   2988936.
  6. Urbonavicius J, Qian Q, Durand JM, Hagervall TG, Björk GR (September 2001). "Improvement of reading frame maintenance is a common function for several tRNA modifications". The EMBO Journal. 20 (17): 4863–4873. doi:10.1093/emboj/20.17.4863. PMC   125605 . PMID   11532950.
  7. Sazinas P, Redgwell T, Rihtman B, Grigonyte A, Michniewski S, Scanlan DJ, et al. (January 2018). "Comparative Genomics of Bacteriophage of the Genus Seuratvirus". Genome Biology and Evolution. 10 (1): 72–76. doi:10.1063/5.0085058.7. PMC   5758909 . PMID   29272407.
  8. Sabri M, Häuser R, Ouellette M, Liu J, Dehbi M, Moeck G, et al. (January 2011). "Genome annotation and intraviral interactome for the Streptococcus pneumoniae virulent phage Dp-1". Journal of Bacteriology. 193 (2): 551–562. doi:10.1128/JB.01117-10. PMC   3019816 . PMID   21097633.

Further reading