The role of the minor base N4-acetylcytidine in the function of the Escherichia coli noninitiator methionine transfer RNA.

Stern, Lawrence A.; Schulman, LaDonne H.

doi:10.1016/s0021-9258(17)34590-8

Cited by 101 publications

(53 citation statements)

References 51 publications

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“…Modifications at base 34 are also essential for accurate codon-anticodon interactions at the ribosome. For example, E. coli tRNA Met CAU lacking its C34 N 4 -acetyl modification was unable to accurately discriminate between AUA and AUG codons (Stern and Schulman, 1978). Our results reinforce the importance of anticodon stem and loop recognition by MpMRS but also point to the acceptor stem as the primary site of tRNA Met CAU and tRNA Ile CAU discrimination by the enzyme.…”

Section: Molecular Cellsupporting

confidence: 67%

“…In E. coli this modification has a four-fold function: it prevents aminoacylation of tRNA Ile CAU by MRS; it allows aminoacylation of the same tRNA by isoleucyl-tRNA synthetase (IRS); it prevents the pairing of tRNA Ile CAU to AUG codons; and it allows the formation of AUA-LAU codon-anticodon pairs. In addition to modification of tRNA Ile CAU , the C34 residue of E. coli tRNA Met CAU is also modified in vivo to N 4 -acetyl-C by an unknown enzyme to prevent it from incorrectly translating isoleucine AUA codons with methionine (Stern and Schulman, 1978).…”

Section: Introductionmentioning

confidence: 99%

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An Operational RNA Code for Faithful Assignment of AUG Triplets to Methionine

et al. 2008

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The assignment of AUG codons to methionine remains a central question of the evolution of the genetic code. We have unveiled a strategy for the discrimination among tRNAs containing CAU (AUG-decoding) anticodons. Mycoplasma penetrans methionyl-tRNA synthetase can directly differentiate between tRNA(Ile)(CAU) and tRNA(Met)(CAU) transcripts (a recognition normally achieved through the modification of anticodon bases). This discrimination mechanism is based only on interactions with the acceptor stems of tRNA(Ile)(CAU) and tRNA(Met)(CAU). Thus, in certain species, the fidelity of translation of methionine codons requires a discrimination mechanism that is independent of the information contained in the anticodon.

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Section: Molecular Cellsupporting

confidence: 67%

Section: Introductionmentioning

confidence: 99%

An Operational RNA Code for Faithful Assignment of AUG Triplets to Methionine

et al. 2008

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“…2,34 In 1977, researchers in E. coli found that ac4C at the wobble position of tRNA Met could help tRNA correctly read codons. 32 In the same year, the researchers detected ac4C at rat hepatocyte 18S rRNA. 37 In 1989, researchers found that ac4C at the wobble position of tRNA Met aided in the correct reading of codons by stabilizing the ribose C3 0 endo conformation in E. coli.…”

Section: Rna Acetylation and Ac4cmentioning

confidence: 99%

The Processing, Gene Regulation, Biological Functions, and Clinical Relevance of N4-Acetylcytidine on RNA: A Systematic Review

Jin

Zou

et al. 2020

Molecular Therapy - Nucleic Acids

143

107

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“…Recently, N4-acetylcytidine (ac4C) has been newly identified as an mRNA modification, which is also a key determinant of post-transcriptional regulation (Arango et al, 2018). ac4C was initially detected in the bacterial transfer RNA (tRNA) anticodon (Stern and Schulman, 1978) and subsequently described in eukaryotic serine and leucine tRNAs and 18S ribosomal RNAs (rRNA) (Boccaletto and Baginski, 2021). Arango et al (2018) utilized transcriptome-wide approaches and found that ac4C is widely distributed within the human transcriptome with many sites in coding sequences.…”

Section: Introductionmentioning

confidence: 99%

NAT10-Mediated N4-Acetylcytidine of RNA Contributes to Post-transcriptional Regulation of Mouse Oocyte Maturation in vitro

Xiang

Zhou

Guo

et al. 2021

Front. Cell Dev. Biol.

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N4-acetylcytidine (ac4C), a newly identified epigenetic modification within mRNA, has been characterized as a crucial regulator of mRNA stability and translation efficiency. However, the role of ac4C during oocyte maturation, the process mainly controlled via post-transcriptional mechanisms, has not been explored. N-acetyltransferase 10 (NAT10) is the only known enzyme responsible for ac4C production in mammals and ac4C-binding proteins have not been reported yet. In this study, we have documented decreasing trends of both ac4C and NAT10 expression from immature to mature mouse oocytes. With NAT10 knockdown mediated by small interfering RNA (siRNA) in germinal vesicle (GV)-stage oocytes, ac4C modification was reduced and meiotic maturation in vitro was significantly retarded. Specifically, the rate of first polar body extrusion was significantly decreased with NAT10 knockdown (34.6%) compared to control oocytes without transfection (74.6%) and oocytes transfected with negative control siRNA (72.6%) (p < 0.001), while rates of germinal vesicle breakdown (GVBD) were not significantly different (p = 0.6531). RNA immunoprecipitation and high-throughput sequencing using HEK293T cells revealed that the modulated genes were enriched in biological processes associated with nucleosome assembly, chromatin silencing, chromatin modification and cytoskeletal anchoring. In addition, we identified TBL3 as a potential ac4C-binding protein by a bioinformatics algorithm and RNA pulldown with HEK293T cells, which may mediate downstream cellular activities. Taken together, our results suggest that NAT10-mediated ac4C modification is an important regulatory factor during oocyte maturation in vitro and TBL3 is a potential ac4C-binding protein.

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The role of the minor base N4-acetylcytidine in the function of the Escherichia coli noninitiator methionine transfer RNA.

Cited by 101 publications

References 51 publications

An Operational RNA Code for Faithful Assignment of AUG Triplets to Methionine

An Operational RNA Code for Faithful Assignment of AUG Triplets to Methionine

The Processing, Gene Regulation, Biological Functions, and Clinical Relevance of N4-Acetylcytidine on RNA: A Systematic Review

NAT10-Mediated N4-Acetylcytidine of RNA Contributes to Post-transcriptional Regulation of Mouse Oocyte Maturation in vitro

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