Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0026936 (
Mycoplasma
)
14,761
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Phenylalanine tRNA from
Mycoplasma
sp. (Kid) was purified and characterized. The tRNA can be aminoacylated by
phenylalanyl-tRNA synthetase
from both
Mycoplasma
and E. coli. In a tRNA-dependent cell-free E. coli amino acid incorporating system programmed with poly U pure
Mycoplasma
tRNA(Phe) was fully active in promoting phenylalanine incorporation, even in direct competition with homologous E. coli tRNA(Phe). Since the
Mycoplasma
tRNA lacks isopentenyladenosine, or any related hypermodified nucleoside, it appears that the presence of such nucleosides in tRNA is not an absolute requirement for protein synthesis.
...
PMID:The phenylalanine tRNA from Mycoplasma sp. (Kid): a tRNA lacking hypermodified nucleosides functional in protein synthesis. 461 4
Mistranslation can follow two events during protein synthesis: production of non-cognate amino acid:transfer RNA (tRNA) pairs by aminoacyl-tRNA synthetases (aaRSs) and inaccurate selection of aminoacyl-tRNAs by the ribosome. Many aaRSs actively edit non-cognate amino acids, but editing mechanisms are not evolutionarily conserved, and their physiological significance remains unclear. To address the connection between aaRSs and mistranslation, the evolutionary divergence of tyrosine editing by
phenylalanyl-tRNA synthetase
(
PheRS
) was used as a model. Certain PheRSs are naturally error prone, most notably a
Mycoplasma
example that displayed a low level of specificity consistent with elevated mistranslation of the proteome.
Mycoplasma
PheRS
was found to lack canonical editing activity, relying instead on discrimination against the non-cognate amino acid by kinetic proofreading. This mechanism of discrimination is inadequate for organisms where translation is more accurate, as
Mycoplasma
PheRS
failed to support Escherichia coli growth. However, minor changes in the defunct editing domain of the
Mycoplasma
enzyme were sufficient to restore E. coli growth, indicating that translational accuracy is an evolutionarily selectable trait.
...
PMID:Selection of tRNA charging quality control mechanisms that increase mistranslation of the genetic code. 2322 33