Purification, crystallization, and preliminary X-ray diffraction studies of tRNA-guanine transglycosylase fromZymomonas mobilis

Romier, Christophe; Ficner, Ralf; Reuter, Klaus; Suck, Dietrich

doi:10.1002/(sici)1097-0134(199604)24:4<516::aid-prot11>3.0.co;2-o

Cited by 33 publications

(5 citation statements)

References 20 publications

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“…E-mail : suck@embl-heidelberg.de strate for Escherichia coli TGT [23][24][25]. We have recently solved the structure of Zymomonas mobilis TGT, alone and in complex with preQi [20,26,27]. The enzyme adopts a noncanonical (ß/oc) 8 -barrel fold with the preQi-binding pocket located at the C-terminal face of the barrel.…”

Section: Introductionmentioning

confidence: 99%

Slight sequence variations of a common fold explain the substrate specificities of tRNA‐guanine transglycosylases from the three kingdoms

1997

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tRNA-guanine transglycosylases (TGTs) are the enzymes catalyzing the base exchange required for the synthesis of the modified bases derived from 7-deazaguanine in prokaryotic, archaebacterial, and eukaryotic tRNAs. Unlike the eukaryotic and archaebacterial enzymes, the prokaryotic TGTs have been clearly identified and highly characterized both biochemically and structurally. The recent occurrence in sequence databases of archaebacterial and eukaryotic proteins homologous to the prokaryotic TGTs reveals that all TGTs unexpectedly adopt a common fold. Observed sequence variations at the active site correlate well with their specificities for the various 7-deazaguanine derivatives and the total conservation of the catalytic residues strongly favors a common catalytic mechanism for all TGTs.

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Section: Introductionmentioning

confidence: 99%

Slight sequence variations of a common fold explain the substrate specificities of tRNA‐guanine transglycosylases from the three kingdoms

1997

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“…Z mobilis TGT, both wild‐type and S103A mutant, were prepared as described previously [16,20] and stored at 4°C as microcrystalline suspension. Prior to use, a small sample of the microcrystals was redissolved in a high‐salt buffer composed of 10 mM HEPES (pH 7.5), 10 mM MgCl 2 and an appropriate concentration of NaCl.…”

Section: Methodsmentioning

confidence: 99%

“…PreQ 1 was synthesized as described previously [19]. Wild‐type TGT and TGT(S103A) were crystallized as described previously [20]. Crystals were soaked for 3 days at 22°C in a buffer composed of 5% (w/v) PEG 8000, 10% (v/v) DMSO, 100 mM Tris (pH 8.5), 1 mM DTT and 50 mM preQ 1 .…”

Section: Methodsmentioning

confidence: 99%

Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA‐guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity

et al. 1999

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The tRNA modifying enzyme tRNA-guanine transglycosylase (TGT) is involved in the exchange of guanine in the first position of the anticodon with preQ 1 as part of the biosynthesis of the hypermodified base queuine (Q). Mutation of Ser 90 to an alanine in Escherichia coli TGT leads to a dramatic reduction of enzymatic activity (Reuter, K. et al. (1994) Biochemistry 33, 7041^7046). To further clarify the role of this residue in the catalytic center, we have mutated the corresponding Ser 103 of the crystallizable Zymomonas mobilis TGT into alanine. The crystal structure of a TGT(S103A)/preQ 1 complex combined with biochemical data presented in this paper suggest that Ser 103 is essential for substrate orientation in the TGT reaction.z 1999 Federation of European Biochemical Societies.

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“…The crystal structure of the TGT from Z. mobilis has been solved at 1.85 Å, revealing a non-canonical (β/α) 8 -barrel fold [18]. Soaking of the crystals with the preQ 1 substrate allowed for the first identification of the TGT active site [19].…”

Section: Trna-guanine Transgylcosylasementioning

confidence: 99%

Transglycosylation: A mechanism for RNA modification (and editing?)

Garcia

Kittendorf

2005

Bioorganic Chemistry

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The vast majority of the ca. 100 chemically distinct modified nucleosides in RNA appear to arise via the chemical transformation of a genetically encoded nucleoside. Two notable exceptions are queuosine and pseudouridine, which are incorporated into tRNA via transglycosylation. Transglycosylation is an extremely efficient process for incorporating highly modified bases such as queuine into RNA. Transglycosylation is also a requisite process for "isomerizing" an Nnucleoside into a C-nucleoside as is the case for pseudouridine formation. Finally, transglycosylation is an attractive possibility for certain RNA editing events (e.g., pyrimidine to purine conversions) that cannot occur via the known, more straightforward enzymatic reactions (e.g., deaminations). This review discusses what is known about the mechanisms of transglycosylation for the queuine and pseudouridine RNA modifications and will speculate about a potential role for transglycosylation in certain RNA editing events.

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Purification, crystallization, and preliminary X-ray diffraction studies of tRNA-guanine transglycosylase fromZymomonas mobilis

Cited by 33 publications

References 20 publications

Slight sequence variations of a common fold explain the substrate specificities of tRNA‐guanine transglycosylases from the three kingdoms

Slight sequence variations of a common fold explain the substrate specificities of tRNA‐guanine transglycosylases from the three kingdoms

Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA‐guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity

Transglycosylation: A mechanism for RNA modification (and editing?)

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