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Cited by 134RNA and protein synthesis mechanismsBiochemical and Molecular ResearchBacterial Genetics and Biotechnology

When Too Much ATP Is Bad for Protein Synthesis

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Pontes, Mauricio H., Sevostyanova, Anastasia, Groisman, Eduardo A.·2015·Journal of Molecular Biology
DOI 10.1016/j.jmb.2015.06.021PMC PMC4531837
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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 (Mg(2+)), 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 Mg(2+) limitation because ATP is the most abundant nucleotide triphosphate in the cell, and Mg(2+) is also required for the stabilization of the cytoplasmic membrane and as a cofactor for essential enzymes. We propose that organisms cope with Mg(2+) limitation by decreasing ATP levels and ribosome production, thereby reallocating Mg(2+) to indispensable cellular processes.

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  • The intracellular Mg2+ pool (~50-100 mM) is distributed about equally between a large macromolecule-associated pool and a LMW pool.

    “Here, we focus on the intracellular Mg2+ pool (∼50–100 mM), which is distributed about equally between a large, macromolecule-associated pool and a LMW pool.60”

    From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [60]

    The Introduction (Protein synthesis, ATP and Mg2+; page unavailable) says about 50% of total Mg2+ binds nucleotide triphosphates and describes substantial Mg2+ binding to ribosomes and other macromolecules, broadly supporting an approximately equal division between low-molecular-weight and macromolecule-associated pools. But it gives 75–100 mM as total Mg2+ in bacteria, of which only 50–65 mM is intracellular; it does not give 50–100 mM as the intracellular concentration. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Other estimates of the contribution of the ribosome to Mg2+ pools are in the same range, corresponding to ~12 mM in E. coli or as much as ~25% of the quota.

    “Other estimates of the contribution of the ribosome to Mg2+ pools are in this same range, corresponding to ∼12 mM in E. coli(5) or as much as ∼25% of the quota.60”

    From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [60]

  • The LMW Mg2+ pool is dominated by ATP and other NTPs, which bind Mg2+ with relatively high affinity (Kd ~0.1-0.3 mM).

    “The LMW Mg2+ pool is dominated by ATP and other NTPs60 that bind Mg2+ with relatively high affinity (Kd values of ∼0.1–0.3 mM).43”

    From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [60]

  • Cell envelope-associated Mg2+ serves as a counterion for membrane phospholipids and lipopolysaccharides in Gram-negative bacteria and can account for 1/3 of the Mg2+ quota.

    “Cell envelope-associated Mg2+ serves as a counterion for membrane phospholipids and lipopolysaccharides in Gram-negative bacteria and this can account for 1/3 of the quota (Figure 3).60”

    From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [60]

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Authors
Pontes, M. H., Sevostyanova, A., & Groisman, E. A.
Affiliations
  • Howard Hughes Medical Institute (US)
  • Yale University (US)
Corresponding author
Groisman, Eduardo A.
ORCID
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2015-08
Volume
427
Issue
16
Pages
2586-2594
ISSN
0022-2836 (ISSN-L)
DOI
10.1016/j.jmb.2015.06.021
PMC
PMC4531837
OpenAlex
W783132086
Cited by
134
References
2
Citations by year
2026: 15 · 2025: 15 · 2024: 22 · 2023: 21 · 2022: 15 · 2021: 8 · 2020: 8 · 2019: 7 · 2018: 8 · 2017: 6 · 2016: 6 · 2015: 3
FWCI
0.75
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Journal of Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institutes of Health (AI49561)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
adenosine triphosphate, magnesium limitation, protein synthesis, tRNA aminoacylation, ribosome biogenesis, translation initiation, ATP levels, cellular energy metabolism, cofactors
MeSH terms
Adenosine Triphosphate, Energy Metabolism, Escherichia coli, Humans, Magnesium, Ribosomes, Transcription, Genetic, Protein Biosynthesis

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