Escherichia coli methionine-tRNAi/methionyl tRNA synthetase pairs induced protein initiation of interest (PII) expression

نویسندگان

چکیده

Abstract The precise regulatory role in protein synthesis by facilitating interactions with mRNA codons for various tRNA modifications is unclear. We previously reported that enhanced green fluorescent (GFP) reduced GFP expression human methionine-conjugated initiator (tRNAi)/tRNA synthetase pairs under methionine-deficient conditions. Here, we investigated the effect of non-formylated Escherichia coli tRNAi on initiation interest (PII) HeLa cells intracellular L-methionine levels. found E. methionine-tRNAi counteracts methionine-tRNAi, indicating methionyl can induce due to increased stability mRNA. Both complexes could support translation without being employed introduce methionine residues subsequent elongation steps. results indicated offset and methionine-tRNAi/methionyl drive expression. Unlike were used as a positive control, mRNA, resulting cell survival. Using tRNAs functions causes heterologous origin, such from prokaryotes, modified, enhance or suppress specific proteins eukaryotic organisms into potential may possess more prominent advantage approaches control PII. This study provides new insights methionine- tRNAi/methionyl pair induced PII relative viability pave way regulate ecological/biological systems.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Control of Escherichia coli lysyl-tRNA synthetase expression by anaerobiosis.

Escherichia coli lysyl-tRNA synthetase was previously shown to occur as two distinct species encoded by either the lysS or the lysU gene. The expression of one of these genes, lysU, is under the control of cell growth conditions. To study the regulation of lysU, delta lysS strains were constructed. During aerobic growth at 37 degrees C or below, the amount of the lysU product in the cell is so ...

متن کامل

Valyl-tRNA Synthetase Gene of Escherichia coli

We report the subcloning and characterization of the molecular elements necessary for the expression of the Escherichia coli valS gene which encodes the enzyme valyl-tRNA synthetase (EC 6.1.1.9). The valS gene was subcloned from the Clarke-Carbon plasmid pLC26-22 by genetic complementation of the valS temperature-sensitive mutant strain, AB4 141. The protein-coding region of the valS struct...

متن کامل

Regulation of lysyl-tRNA synthetase expression by histone-like protein H-NS of Escherichia coli.

The lysU gene encoding lysyl-tRNA synthetase of Escherichia coli is normally silent at low temperatures and is expressed by certain metabolites and stimuli. A novel class of lysU-constitutive mutations were isolated by random insertion mutagenesis. These mutations nullified the hns gene encoding a histone-like protein, H-NS, and affected thermoregulation of lysU.

متن کامل

Evolution of multiple, mutually orthogonal prolyl-tRNA synthetase/tRNA pairs for unnatural amino acid mutagenesis in Escherichia coli.

The site-specific incorporation of unnatural amino acids (UAAs) into proteins in living cells relies on an engineered tRNA/aminoacyl-tRNA synthetase (tRNA/aaRS) pair, orthogonal to the host cell, to deliver the UAA of choice in response to a unique nonsense or frameshift codon. Here we report the generation of mutually orthogonal prolyl-tRNA/prolyl-tRNA synthase (ProRS) pairs derived from an ar...

متن کامل

Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant.

The Escherichia coli tls-1 strain carrying a mutated aspS gene (coding for aspartyl-tRNA synthetase), which causes a temperature-sensitive growth phenotype, was cloned by PCR, sequenced, and shown to contain a single mutation resulting in substitution by serine of the highly conserved proline 555, which is located in motif 3. When an aspS fragment spanning the codon for proline 555 was transfor...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Applied Biological Chemistry

سال: 2022

ISSN: ['2468-0834', '2468-0842']

DOI: https://doi.org/10.1186/s13765-022-00748-0