Evidence map›Paper›PMID 28812634›Full record

ArticleNature ecology & evolution2017

Optimization of lag phase shapes the evolution of a bacterial enzyme.

Bharat V Adkar, Michael Manhart, Sanchari Bhattacharyya, Jian Tian, Michael Musharbash, Eugene I Shakhnovich

Abstract read
In one paragraph

Article in Nature ecology & evolution, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
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  5. Understanding cellular growth strategies via optimal control.Journal of the Royal Society, Interface · 2023
    Article
  6. Article
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  8. The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021
    Review
  9. Article
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  15. Article
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  17. Substrate inhibition imposes fitness penalty at high protein stability.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Review
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  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 2 countries.

Bharat V AdkarDepartment of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA.ORCID http://orcid.org/0000-0002-9168-051X
Michael ManhartDepartment of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA.ORCID http://orcid.org/0000-0003-3791-9056
Sanchari BhattacharyyaDepartment of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA.ORCID http://orcid.org/0000-0003-3421-4755
Jian TianDepartment of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA.
Michael MusharbashDepartment of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA.
Eugene I ShakhnovichDepartment of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA.ORCID http://orcid.org/0000-0002-4769-2265
Harvard University · US

Funding

Study of Biological Evolution of Structure and Function in ProteinsR01GM068670 · NIGMS · HARVARD UNIVERSITY · PI SHAKHNOVICH, EUGENE I · 2004 to 2020
$7.0M
Characterizing the Co-evolution of Protein-protein and Regulatory InteractionsF32GM116217 · NIGMS · HARVARD UNIVERSITY · PI MANHART, MICHAEL · 2015 to 2017
$168k
NIGMS NIH HHS F32 GM116217NIGMS NIH HHS R01 GM068670
6 · The paper itself

Abstract

Mutations provide the variation that drives evolution, yet their effects on fitness remain poorly understood. Here we explore how mutations in the essential enzyme adenylate kinase (Adk) of Escherichia coli affect multiple phases of population growth. We introduce a biophysical fitness landscape for these phases, showing how they depend on molecular and cellular properties of Adk. We find that Adk catalytic capacity in the cell (the product of activity and abundance) is the major determinant of mutational fitness effects. We show that bacterial lag times are at a well-defined optimum with respect to Adk's catalytic capacity, while exponential growth rates are only weakly affected by variation in Adk. Direct pairwise competitions between strains show how environmental conditions modulate the outcome of a competition where growth rates and lag times have a tradeoff, shedding light on the multidimensional nature of fitness and its importance in the evolutionary optimization of enzymes.

Identifiers

PMID28812634
PMCPMC5640271
OpenAlexW2950293442

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.