When Too Much ATP Is Bad for Protein Synthesis

Mauricio H. Pontes, Anastasia Sevostyanova, Eduardo A. Groisman

Research output: Contribution to journalReview articlepeer-review

33 Scopus citations

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

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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