tRNA‐like structures

Mans, R. M. W.; Pleij, C.W.A.; Bosch, L.

doi:10.1111/j.1432-1033.1991.tb16288.x

Cited by 122 publications

(96 citation statements)

References 229 publications

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“…The RNA of the turnip yellow mosaic virus (TYMV) is aminoacylated with valine by ValRS from yeast as well as with histidine by HisRS, albeit with lower efficiency (Rudinger et al, 1992). This indicates that the TYMV RNA contains essential identity elements recognized by both aaRS enzymes (for compilations see also Mans et al, 1991;Giegé, 1996). Furthermore, the Brome mosaic virus RNA possesses a tRNA-like domain that is aminoacylated with tyrosine, valine, and histidine by the corresponding aaRS from yeast (Felden et al, 1994.…”

Section: Identity Of Trna Hismentioning

confidence: 99%

Histidyl-tRNA Synthetase

Freist¹,

Jf²,

Rühlmann³

et al. 1999

Biological Chemistry

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Histidyl-tRNA synthetase (HisRS) is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. This amino acid has uniquely moderate basic properties and is an important group in many catalytic functions of enzymes.A compilation of currently known primary structures of HisRS shows that the subunits of these homodimeric enzymes consist of 420 -550 amino acid residues. This represents a relatively short chain length among aminoacyl-tRNA synthetases (aaRS), whose peptide chain sizes range from about 300 to 1100 amino acid residues.The crystal structures of HisRS from two organisms and their complexes with histidine, histidyl-adenylate and histidinol with ATP have been solved. HisRS from Escherichia coli and Thermus thermophilus are very similar dimeric enzymes consisting of three domains: the N-terminal catalytic domain containing the sixstranded antiparallel ␤-sheet and the three motifs characteristic of class II aaRS, a HisRS-specific helical domain inserted between motifs 2 and 3 that may contact the acceptor stem of the tRNA, and a C-terminal ␣/␤ domain that may be involved in the recognition of the anticodon stem and loop of tRNA His .The aminoacylation reaction follows the standard two-step mechanism. HisRS also belongs to the group of aaRS that can rapidly synthesize diadenosine tetraphosphate, a compound that is suspected to be involved in several regulatory mechanisms of cell metabolism. Many analogs of histidine have been tested for their properties as substrates or inhibitors of HisRS, leading to the elucidation of structure-activity relationships concerning configuration, importance of the carboxy and amino group, and the nature of the side chain.HisRS has been found to act as a particularly important antigen in autoimmune diseases such as rheumatic arthritis or myositis. Successful attempts have been made to identify epitopes responsible for the complexation with such auto-antibodies.

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Section: Identity Of Trna Hismentioning

confidence: 99%

Histidyl-tRNA Synthetase

Freist¹,

Jf²,

Rühlmann³

et al. 1999

Biological Chemistry

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“…1 (a). The most interesting feature of this folding is the close similarity of the structure formed by the last 186 3'-terminal nucleotides to that proposed for the 3'-UTR of tobacco mosaic virus (TMV) and other tobamoviruses (van Belkum et al, 1985;Pleij et al, 1987;Mans et al, 1991), shown in Fig. 1 (b).…”

mentioning

confidence: 99%

“…This structure is very 0001-2459 © 1994 SGM (van Belkum et al, 1985;Pleij et al, 1987;Garcia-Arenal, 1988;Mans et al, 1991) with one exception, RNA from the valine-accepting cowpea strain of TMV. The latter adopts a tRNA-like structure that is closely related to that of valine-accepting tymoviral RNAs (Meshi et al, 1981).…”

mentioning

confidence: 99%

“…The tRNA-like structure, which is present in a number of RNAs from various plant viruses, including tobamoviruses, was shown to be necessary for aminoacylation (for a review see Mans et at., 1991). This structure is very 0001-2459 © 1994 SGM (van Belkum et al, 1985;Pleij et al, 1987;Garcia-Arenal, 1988;Mans et al, 1991) with one exception, RNA from the valine-accepting cowpea strain of TMV.…”

mentioning

confidence: 99%

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Similarities between the secondary structure of satellite tobacco mosaic virus and tobamovirus RNAs

Gultyaev

Batenburg

Pleij

1994

Journal of General Virology

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“…Such features may include the ability to recognize a tRNA with a long variable arm in a specific orientation that matches P7 and the flexibly hinged C-terminal domain, which may facilitate the binding of some non-tRNA substrates. The latter may include not only group I introns but also the 3Ј-terminal tRNA-like structures of RNA viruses (33). In addition, CYT-18 contains several idiosyncratic insertions and an extended C-terminal domain, which may contribute to splicing via unique interactions with group I introns.…”

Section: Discussionmentioning

confidence: 99%

tRNA-like recognition of group I introns by a tyrosyl-tRNA synthetase

Myers

Kuhla

Cusack

et al. 2002

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

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The Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) functions in splicing group I introns by promoting the formation of the catalytically active RNA structure. Previous work suggested that CYT-18 recognizes a conserved tRNA-like structure of the group I intron catalytic core. Here, directed hydroxyl-radical cleavage assays show that the nucleotide-binding fold and C-terminal domains of CYT-18 interact with the expected group I intron cognates of the aminoacyl-acceptor stem and Danticodon arms, respectively. Further, three-dimensional graphic modeling, supported by biochemical data, shows that conserved regions of group I introns can be superimposed over interacting regions of the tRNA in a Thermus thermophilus TyrRS͞tRNA Tyr cocrystal structure. Our results support the hypothesis that CYT-18 and other aminoacyl-tRNA synthetases interact with group I introns by recognizing conserved tRNA-like structural features of the intron RNAs.T he Neurospora crassa mitochondrial (mt) tyrosyl-tRNA synthetase (TyrRS), or CYT-18 protein, functions in both tRNA Tyr aminoacylation and group I intron splicing (1). The splicing function reflects that CYT-18 recognizes conserved structural features of group I intron and promotes the formation of the catalytically active RNA structure (2-5). Group I introns, similar to tRNAs, have minimal sequence conservation but share a conserved three-dimensional structure consisting of two double-helical domains (6, 7). The group I intron's P4-P6 domain is formed by the coaxial stacking of secondary structure elements P5, P4, P6, and P6a, and the P3-P9 domain is formed by P3, P8, P7, and P9, with the juxtaposition of the two domains creating a cleft that contains the intron's active site. RNA-footprinting experiments with the CYT-18-dependent N. crassa mt large subunit rRNA (LSU) and ND1 introns showed that the protein interacts with the phosphodiester backbone on the side opposite the active-site cleft, with most of the potential contact sites in the P4-P6 domain and a few additional sites in the P3-P9 domain (4, 5). Biochemical and genetic studies led to a model in which CYT-18 binds first to the P4-P6 domain to promote its assembly and then makes additional contacts with the P3-P9 domain to stabilize the two domains in the correct relative orientation to form the intron's active site (4,5,(8)(9)(10).Remarkably, comparison of the CYT-18 binding sites in the N. crassa mt LSU and ND1 introns with that in the N. crassa mt tRNA Tyr by graphic modeling revealed an extended threedimensional overlap between the tRNA and highly conserved regions of the group I intron catalytic core (5). In this overlap, the group I intron's P4-P6 stacked helices almost completely superimpose on the tRNA's D-anticodon arm stacked helices, P7 overlaps the variable arm, and P9 largely parallels the acceptor stem, with the discriminator base directly overlapping L9-1, a putative protein contact site in both RNAs. These structural similarities suggest that aminoacyl-tRNA synthetases (aaRSs) and othe...

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tRNA‐like structures

Cited by 122 publications

References 229 publications

Histidyl-tRNA Synthetase

Histidyl-tRNA Synthetase

Similarities between the secondary structure of satellite tobacco mosaic virus and tobamovirus RNAs

tRNA-like recognition of group I introns by a tyrosyl-tRNA synthetase

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