Old enzymes versus new herbicides

Hendrickson, Tamara L.

doi:10.1074/jbc.h118.002878

Cited by 2 publications

(4 citation statements)

References 10 publications

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“…145,146 Instead of hydrolyzing Gln or Asn to release ammonia, AtzE hydrolyzes 1-carboxybiuret to 1,3-dicarboxyurea. 145,146 AtzG helps to stabilize AtzE by forming an AtxEG complex. 145,146 The E-subunit of GatDE is a homolog of GatB (Figure 5B).…”

Section: The Trna-dependent Amidotransferases: Gatcab and Gatdementioning

confidence: 99%

“…145,146 AtzG helps to stabilize AtzE by forming an AtxEG complex. 145,146 The E-subunit of GatDE is a homolog of GatB (Figure 5B). 23,40,132,133 Accordingly, it is the kinase and tRNA-binding domain of the archaeal Glu-AdT.…”

Section: The Trna-dependent Amidotransferases: Gatcab and Gatdementioning

confidence: 99%

“…GatC and GatA homologs (AtzG and AtzE, respectively) have evolved in bacteria, like a Pseudomonas sp. strain, to be involved in a vital step in the degradation of the herbicide atrazine 145,146 . Instead of hydrolyzing Gln or Asn to release ammonia, AtzE hydrolyzes 1‐carboxybiuret to 1,3‐dicarboxyurea 145,146 .…”

Section: The Trna‐dependent Amidotransferases: Gatcab and Gatdementioning

confidence: 99%

“…strain, to be involved in a vital step in the degradation of the herbicide atrazine 145,146 . Instead of hydrolyzing Gln or Asn to release ammonia, AtzE hydrolyzes 1‐carboxybiuret to 1,3‐dicarboxyurea 145,146 . AtzG helps to stabilize AtzE by forming an AtxEG complex 145,146 …”

Section: The Trna‐dependent Amidotransferases: Gatcab and Gatdementioning

confidence: 99%

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Evolution and variation in amide aminoacyl‐tRNA synthesis

Lewis,

Fallon,

Dittemore

et al. 2024

IUBMB Life

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The amide proteogenic amino acids, asparagine and glutamine, are two of the twenty amino acids used in translation by all known life. The aminoacyl‐tRNA synthetases for asparagine and glutamine, asparaginyl‐tRNA synthetase and glutaminyl tRNA synthetase, evolved after the split in the last universal common ancestor of modern organisms. Before that split, life used two‐step indirect pathways to synthesize asparagine and glutamine on their cognate tRNAs to form the aminoacyl‐tRNA used in translation. These two‐step pathways were retained throughout much of the bacterial and archaeal domains of life and eukaryotic organelles. The indirect routes use non‐discriminating aminoacyl‐tRNA synthetases (non‐discriminating aspartyl‐tRNA synthetase and non‐discriminating glutamyl‐tRNA synthetase) to misaminoacylate the tRNA. The misaminoacylated tRNA formed is then transamidated into the amide aminoacyl‐tRNA used in protein synthesis by tRNA‐dependent amidotransferases (GatCAB and GatDE). The enzymes and tRNAs involved assemble into complexes known as transamidosomes to help maintain translational fidelity. These pathways have evolved to meet the varied cellular needs across a diverse set of organisms, leading to significant variation. In certain bacteria, the indirect pathways may provide a means to adapt to cellular stress by reducing the fidelity of protein synthesis. The retention of these indirect pathways versus acquisition of asparaginyl‐tRNA synthetase and glutaminyl tRNA synthetase in lineages likely involves a complex interplay of the competing uses of glutamine and asparagine beyond translation, energetic costs, co‐evolution between enzymes and tRNA, and involvement in stress response that await further investigation.

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