When Too Much ATP Is Bad for Protein Synthesis

Mauricio Henriques Pontes, Anastasia Sevostyanova, Eduardo A. Groisman

Research output: Contribution to journalReview article

23 Citations (Scopus)

Abstract

Abstract Adenosine triphosphate (ATP) is the energy currency of living cells. Even though ATP powers virtually all energy-dependent activities, most cellular ATP is utilized in protein synthesis via tRNA aminoacylation and guanosine triphosphate regeneration. Magnesium (Mg2+), the most common divalent cation in living cells, plays crucial roles in protein synthesis by maintaining the structure of ribosomes, participating in the biochemistry of translation initiation and functioning as a counterion for ATP. A non-physiological increase in ATP levels hinders growth in cells experiencing Mg2+ limitation because ATP is the most abundant nucleotide triphosphate in the cell, and Mg2+ is also required for the stabilization of the cytoplasmic membrane and as a cofactor for essential enzymes. We propose that organisms cope with Mg2+ limitation by decreasing ATP levels and ribosome production, thereby reallocating Mg2+ to indispensable cellular processes.

Original languageEnglish (US)
Article number64790
Pages (from-to)2586-2594
Number of pages9
JournalJournal of Molecular Biology
Volume427
Issue number16
DOIs
StatePublished - Jul 31 2015

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bcl-Associated Death Protein
Adenosine Triphosphate
Ribosomes
Transfer RNA Aminoacylation
Coenzymes
Divalent Cations
Guanosine Triphosphate
Biochemistry
Magnesium
Regeneration
Proteins
Nucleotides
Cell Membrane

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Cite this

Pontes, Mauricio Henriques ; Sevostyanova, Anastasia ; Groisman, Eduardo A. / When Too Much ATP Is Bad for Protein Synthesis. In: Journal of Molecular Biology. 2015 ; Vol. 427, No. 16. pp. 2586-2594.
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Pontes, MH, Sevostyanova, A & Groisman, EA 2015, 'When Too Much ATP Is Bad for Protein Synthesis', Journal of Molecular Biology, vol. 427, no. 16, 64790, pp. 2586-2594. https://doi.org/10.1016/j.jmb.2015.06.021

When Too Much ATP Is Bad for Protein Synthesis. / Pontes, Mauricio Henriques; Sevostyanova, Anastasia; Groisman, Eduardo A.

In: Journal of Molecular Biology, Vol. 427, No. 16, 64790, 31.07.2015, p. 2586-2594.

Research output: Contribution to journalReview article

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AB - Abstract Adenosine triphosphate (ATP) is the energy currency of living cells. Even though ATP powers virtually all energy-dependent activities, most cellular ATP is utilized in protein synthesis via tRNA aminoacylation and guanosine triphosphate regeneration. Magnesium (Mg2+), the most common divalent cation in living cells, plays crucial roles in protein synthesis by maintaining the structure of ribosomes, participating in the biochemistry of translation initiation and functioning as a counterion for ATP. A non-physiological increase in ATP levels hinders growth in cells experiencing Mg2+ limitation because ATP is the most abundant nucleotide triphosphate in the cell, and Mg2+ is also required for the stabilization of the cytoplasmic membrane and as a cofactor for essential enzymes. We propose that organisms cope with Mg2+ limitation by decreasing ATP levels and ribosome production, thereby reallocating Mg2+ to indispensable cellular processes.

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