Naturally Occurring Isoleucyl-tRNA Synthetase without tRNA-dependent Pre-transfer Editing

Autor: Nikolina Sostaric, Boris Lenhard, Nevena Cvetesic, Ita Gruić-Sovulj, Morana Dulic, Mirna Bilus
Rok vydání: 2015
Předmět:
0301 basic medicine
antibiotic resistance
protein synthesis
Biochemistry
chemistry.chemical_compound
RNA
Transfer

proofreading
PSEUDOMONIC ACID
Genetics
biology
tRNA-dependent pre-transfer editing
11 Medical And Health Sciences
Genetic code
AMINO-ACID
ESCHERICHIA-COLI
Protein Synthesis and Degradation
Transfer RNA
Proofreading
Eukaryote
03 Chemical Sciences
Life Sciences & Biomedicine
STRUCTURAL BASIS
Isoleucine-tRNA Ligase
Biochemistry & Molecular Biology
Isoleucine—tRNA ligase
GENETIC-CODE
MECHANISMS
03 medical and health sciences
QUALITY-CONTROL
Escherichia coli
protein evolution
Molecular Biology
Gene
mupirocin
isoleucyl-tRNA synthetase
pre-transfer editing
eukaryotes
Science & Technology
COMPLEX
Aminoacyl tRNA synthetase
aminoacyl tRNA synthetase
Genetic Complementation Test
RECOGNITION
Streptomyces griseus
MUPIROCIN RESISTANCE
Cell Biology
06 Biological Sciences
biology.organism_classification
transfer RNA (tRNA)
030104 developmental biology
chemistry
Zdroj: The Journal of Biological Chemistry
ISSN: 1083-351X
Popis: Isoleucyl-tRNA synthetase (IleRS) is unusual among aminoacyl-tRNA synthetases in having a tRNA-dependent pre-transfer editing activity. Alongside the typical bacterial IleRS (such as Escherichia coli IleRS), some bacteria also have the enzymes (eukaryote-like) that cluster with eukaryotic IleRSs and exhibit low sensitivity to the antibiotic mupirocin. Our phylogenetic analysis suggests that the ileS1 and ileS2 genes of contemporary bacteria are the descendants of genes that might have arisen by an ancient duplication event before the separation of bacteria and archaea. We present the analysis of evolutionary constraints of the synthetic and editing reactions in eukaryotic/eukaryote-like IleRSs, which share a common origin but diverged through adaptation to different cell environments. The enzyme from the yeast cytosol exhibits tRNA-dependent pre-transfer editing analogous to E. coli IleRS. This argues for the presence of this proofreading in the common ancestor of both IleRS types and an ancient origin of the synthetic site-based quality control step. Yet surprisingly, the eukaryote-like enzyme from Streptomyces griseus IleRS lacks this capacity; at the same time, its synthetic site displays the 10(3)-fold drop in sensitivity to antibiotic mupirocin relative to the yeast enzyme. The discovery that pre-transfer editing is optional in IleRSs lends support to the notion that the conserved post-transfer editing domain is the main checkpoint in these enzymes. We substantiated this by showing that under error-prone conditions S. griseus IleRS is able to rescue the growth of an E. coli lacking functional IleRS, providing the first evidence that tRNA-dependent pre-transfer editing in IleRS is not essential for cell viability.
Databáze: OpenAIRE