Highlights on Trypanosomatid Aminoacyl-tRNA Synthesis
Aminoacyl-tRNA synthetases aaRSs are responsible for the aminoacylation of tRNAs in the first step of protein synthesis. They comprise a group of enzymes that catalyze the formation of each possible aminoacyl-tRNA necessary for messenger RNA decoding in a
- PDF / 716,571 Bytes
- 34 Pages / 439.37 x 666.14 pts Page_size
- 97 Downloads / 160 Views
Highlights on Trypanosomatid Aminoacyl-tRNA Synthesis Carla Polycarpo
Abstract Aminoacyl-tRNA synthetases aaRSs are responsible for the aminoacylation of tRNAs in the first step of protein synthesis. They comprise a group of enzymes that catalyze the formation of each possible aminoacyl-tRNA necessary for messenger RNA decoding in a cell. These enzymes have been divided into two classes according to structural features of their active sites and, although each class shares a common active site core, they present an assorted array of appended domains that makes them sufficiently diverse among the different living organisms. Here we will explore what is known about the diversity encountered among trypanosomatids’ aaRSs that has helped us not only to understand better the biology of these parasites but can be used rationally for the design of drugs against these protozoa.
Abbreviations A aa-AMP aaRS aa-tRNA AC1
Adenine aaRS, 4, 5 aminoacyl-adenylate complexed with aminoacyl-tRNA synthetase Aminoacyl-tRNA synthetase Aminoacyl-tRNA Anticodon binding motif
C. Polycarpo (*) Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil Avenida Carlos Chagas Filho, 373, Centro de Ciências da Saúde, Bloco D, subsolo, sala 5, Cidade Universitária Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular, Rio de Janeiro, RJ 21941-902, Brazil e-mail: [email protected] A.L.S. Santos et al. (eds.), Proteins and Proteomics of Leishmania and Trypanosoma, Subcellular Biochemistry 74, DOI 10.1007/978-94-007-7305-9_12, © Springer Science+Business Media Dordrecht 2014
271
272
AC2 AIDQ AlaRS AMP Arg ArgRS Asn AsnRS Asp AspRS ATP AUA AUG C CPK Cys CysRS E E. coli eEFSec EMAP II-like domain ESE fmet FTHF G GatCAB GatDE GatFAB GLDQ Gln GlnRS Glu GluRS Gly GlyRS GTP GXDQ H HAM
C. Polycarpo
Anticodon binding motif TrpRS and TyrRS motif present in the catalytic site (alanine, isoleucine, aspartate, glutamine) Alanyl-tRNA synthetase Adenosine-5′-monophosphate Arginine Arginyl-tRNA synthetase Asparagine Asparaginyl-tRNA synthetase Aspartate Aspartyl-tRNA synthetase Adenosine-5′-triphosphate Isoleucine codon Methionine codon Cytosine Coloring convention designed by Robert Corey and Linus Pauling, and improved by Walter Koltun. Cysteine Cysteinyl-tRNA synthetase Glutamate Escherichia coli Selenocysteine elongation factor Endothelial monocyte-activating polypeptide II-like domain Eukaryotic specific extension present in TryptophanyltRNA synthetases Formylmethionine N10-formyltetrahydrofolate Guanine tRNA dependent amidotransferase of Archaea, bacteria and eukaryotic organelles Archaeal specific tRNA dependent amidotransferase Yeast specific tRNA dependent amidotransferase Trypanosomatid TyrRS motif present in the catalytic site (glycine, leucine, aspartate, glutamine) Glutamine Glutaminyl-tRNA synthetase Glutamate Glutamyl-tRNA synthetase Glycine Glycyl-tRNA synthetase Guanosine-5′-triphosphate TrpRS motif present in bacteria (glycine, any amino acid, aspartate, glutamine) Histidine
Data Loading...
