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Topic: Aminoacylates

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Transfer RNA

Protein synthesis

	Amino Acid Selectivity in the Aminoacylation of Coenzyme A and RNA Minihelices by Aminoacyl-tRNA Synthetases -- ...
		(14) are substrates for aminoacylations by cognate AARSs, albeit
		aminoacylations of CoA-SH with valine and leucine occurred at
		is consistent with the notion that the aminoacylation of thioesters
	www.jbc.org /cgi/content/full/275/45/34845 (2615 words)

	Suga Laboratory Research: r24 (Site not responding. Last check: 2007-10-13)
		Although this ribozyme is an effective single-turnover catalyst for tRNA aminoacylation, its multiple-turnover ability is inherently limited due to slow dissociation of the ribozyme from tRNA.
		This ribozyme-based aminoacylation system has significant potential to be a powerful and practical technique for supplying various non-natural aminoacyl-tRNAs for a highly efficient in vitro translation system.
		Saito, H. Suga (2001) “A ribozyme aminoacylates exclusively on the 3’-hydroxyl group of the 3’-terminus of tRNA”, J.
	www.acsu.buffalo.edu /~hsuga/r24.html (494 words)

	Expanding the Genetic Code of Escherichia coli Science v.292 20apr01 (Site not responding. Last check: 2007-10-13)
		This synthetase must aminoacylate the rRNA with only the desired unnatural amino acid and none of the common 20 amino acids.
		Likewise, the unnatural amino acid cannot be a substrate for the endogenous synthetases.
		The orthogonal nature of the resulting suppressor tRNAs was tested by an in vivo complementation assay, which is based on suppression of an amber stop codon at a nonessential position (Ala' 84) of the TEM-l (3-lactamase gene carried on plasmid pBLAM.
	www.mindfully.org /GE/GE2/Escherichia-Coli-Code.htm (2813 words)

	PANTHER - Family Information
		Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold and are mostly monomeric [PMID:10673435], while class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet formation, flanked by alpha-helices [PMID:8364025], and are mostly dimeric or multimeric.
		In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred.
		The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine belong to class I synthetases.
	www.pantherdb.org /panther/family.do?clsAccession=PTHR10218:SF2 (323 words)

	SVIBOR - Papers - project code: 1-08-070
		However, from it is preferenceof aminoacylation at 2-OH over 3-OH, it would, like E. coli TyrRSseem to belong to class I. In order to determine the enzyme structure, a S. cerevisiaegenomic expression library were screened with antibodies againstTyrRS.
		The contribution of particular amino acid to the specificity of aminoacylation is being analyzed in vivo, by complementation of yeast SES1 null-allele strain and in vitro, after purification of the mutant SerRS enzymes from a yeast overproducing strain.
		The contribution of different amino acid to the specificity of aminoacylation has been analyzed in vivo and in vitro.
	www.mzos.hr /svibor/1/08/070/rad_e.htm (2940 words)

	Rebecca Alexander - Research Interests and Publications
		As this peptide is at the physical interface between functional domains, and as we expect conformational flexibility is important for catalysis, we introduced cysteine residues at positions that we thought would generate a disulfide bond to limit flexibility of this peptide.
		We are excited to have cut the functional communication through a single covalent bond, and will continue to characterize this and other mutants using kinetic assays, spectroscopy, and crystallography.
		One of the amino acids that may be processed this way by MetRS is homocysteine, which lacks the terminal methyl group of methionine.
	www.wfu.edu /academics/chemistry/faculty/RebeccaAlexanderResearch.html (1089 words)

	Aminoacyl tRNA synthetase - Wikipedia, the free encyclopedia
		An aminoacyl tRNA synthetase (aaRS) is an enzyme that catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA.
		The synthetase first binds ATP and the cognate amino acid to form an aminoacyl-adenylate and release inorganic pyrophosphate (PP i
		Class I has two common homologous peptide sequence motifs.
	en.wikipedia.org /wiki/Aminoacyl_tRNA_synthetase (201 words)

	Initiator-Elongator Discrimination in Vertebrate tRNAs for Protein Synthesis -- Drabkin et al. 18 (3): 1459 -- ...
		Aminoacylation levels of mutant tRNAs in COS1 cells.
		Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu.
		Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu.
	mcb.asm.org /cgi/content/full/18/3/1459 (5559 words)

	Eurekah - Isoleucyl-tRNA Synthetases
		The fidelity of protein synthesis depends on specific tRNA aminoacylation by aminoacyl- tRNA synthetase enzymes, which in turn depend on the recognition of the identity of particular nucleotides...
		It is responsible for aminoacylating the aliphatic amino acid le...
		To scientists in the field, the aminoacyl -RNA synthetases are the greatest of all proteins.
	www.eurekah.com /chapter/1886 (987 words)

	Pfam 20.0 : tRNA-synt_1c (Site not responding. Last check: 2007-10-13)
		In some organisms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
		The aminoacyl-tRNA synthetases () catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction.
		Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold and are mostly monomeric PUBMED:10673435, while class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet formation, flanked by alpha-helices PUBMED:8364025, and are mostly dimeric or multimeric.
	pfam.wustl.edu /cgi-bin/getdesc?name=tRNA-synt_1c (656 words)

	Functional Replacement of Hamster Lysyl-tRNA Synthetase by the Yeast Enzyme Requires Cognate Amino Acid Sequences for ... (Site not responding. Last check: 2007-10-13)
		The yeast and mammalian enzymes, overexpressed in yeast, were purified to homogeneity.
		The 152-aa C-terminus extremity of the hamster enzyme provides the yeast enzyme with the capacity to complement Lys-101 cells.
		This hybrid protein is fairly stable and aminoacylates both yeast and mammalian tRNA
	pubs.acs.org /cgi-bin/abstract.cgi/bichaw/1996/35/i48/abs/bi9617926.html (315 words)

	InterPro: IPR004524 Aspartyl-tRNA synthetase bacterial/mitochondrial type (Site not responding. Last check: 2007-10-13)
		Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold and are mostly monomeric [ 2 ], while class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet formation, flanked by alpha-helices [ 3 ], and are mostly dimeric or multimeric.
		Sugiura I. Nureki O. Ugaji-Yoshikawa Y. Kuwabara S. Shimada A. Tateno M. Lorber B. Giege R. Moras D. Yokoyama S. Konno M. The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules.
		Perona J.J. Rould M.A. Steitz T.A. Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.
	www.ebi.ac.uk /interpro/IEntry?ac=IPR004524 (3435 words)

	Rebecca Alexander's Research Interest and Publications
		acceptor stem is sequence-specifically aminoacylated by MetRS, although the catalytic efficiency of the reaction is significantly decreased. Both the microhelix
		and an anticodon stem-loop mimic bind to MetRS, but the presence of the anticodon stem-loop does not increase the rate of microhelix aminoacylation. At a minimum, therefore, the two portions of tRNA
		Schimmel and R.W. Alexander (1998) "Diverse RNA substrates for aminoacylation: clues to origins?" Proc.
	www.wfu.edu /academics/chemistry/faculty/alex-pub.html (583 words)

	Identity Elements of Archaeal tRNA -- Mallick et al. 12 (4): 235 -- DNA Research
		Sherman, J. M., Rogers, M. J., Soll, D. 1992, Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation, Nucleic Acids Res.
		Hou, Y. and Schimmel, P. 1989, Modeling of in vitro kinetic parameters for the elaboration of transfer RNA identity in vivo, Biochemistry, 28, 4942–4947.
		structure and on its aminoacylation by glutamyl-tRNA synthetase, Eur.
	dnaresearch.oxfordjournals.org /cgi/content/full/12/4/235 (3124 words)

	Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyrRS) and an engineered TyrRS specific for ...
		A structural comparison of all class I aminoacyl RS’s
		conserved mechanism of aminoacyl adenylation among TyrRS (Yaremchuk et al.
		Delagoutte, B., Moras, D., and Cavarelli, J. tRNA aminoacylation by arginyl-tRNA synthetase: Induced conformations during substrates binding.
	protsci.highwire.org /cgi/content/full/14/5/1340 (4619 words)

	Human mitochondrial TyrRS disobeys the tyrosine identity rules -- BONNEFOND et al. 11 (5): 558 -- RNA
		Keywords: tRNA identity; cross-species aminoacylation; phylogeny; tRNA acceptor stem; tyrosylation
		Received November 22, 2004 ; accepted January 14, 2005.
		Loss of a Primordial Identity Element for a Mammalian Mitochondrial Aminoacylation System
	www.rnajournal.org /cgi/content/abstract/11/5/558 (244 words)

	Spiroplasma citri UGG and UGA tryptophan codons: sequence of the two tryptophanyl-tRNAs and organization of the ...
		tRNA(Trp) species can be aminoacylated by using an aminoacyl-tRNA
		from Escherichia coli aminoacylates tRNA(Trp) (CCA) but not
		This article has been cited by other articles:
	jb.asm.org /cgi/content/abstract/174/20/6471 (230 words)

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