Evidence map›Paper›PMID 18314964›Full record

ArticleBiochemistry2008

Importance of the maintenance pathway in the regulation of the activity of Escherichia coli ribonucleotide reductase.

Daniela Hristova, Chia-Hung Wu, Wei Jiang, Carsten Krebs, JoAnne Stubbe

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Bacterial iron detoxification at the molecular level.The Journal of biological chemistry · 2020
    Review
  3. Review
  4. Article
  5. Evidence that a respiratory shield inThe Journal of biological chemistry · 2019
    Article
  6. ISCA1 is essential for mitochondrial FeNature communications · 2017
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
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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

5 authors at 2 institutions in 1 country.

Daniela HristovaDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Chia-Hung Wu
Wei Jiang
Carsten Krebs
JoAnne Stubbe
Pennsylvania State University · USMassachusetts Institute of Technology · US

Funding

Ribonucleotide Reductase: Structure and FunctionR01GM029595 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI STUBBE, JOANNE · 1985 to 2016
$6.9M
MECHANISM OF DINUCLEAR FE-Y. FORMATION OF NDP REDUCTASER37GM029595 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI STUBBE, JOANNE · 1988 to 1997
–
NIGMS NIH HHS GM29595
6 · The paper itself

Abstract

Ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides to deoxynucleotides in all organisms. The Escherichia coli class Ia RNR is composed of alpha and beta subunits that form an alpha 2beta 2 active complex. beta contains the diferric tyrosyl radical (Y (*)) cofactor that is essential for the reduction process that occurs on alpha. [Y (*)] in vitro is proportional to RNR activity, and its regulation in vivo potentially represents a mechanism for controlling RNR activity. To examine this thesis, N- and C-terminal StrepII-tagged beta under the control of an l-arabinose promoter were constructed. Using these constructs and with [ l-arabinose] varying from 0 to 0.5 mM in the growth medium, [beta] could be varied from 4 to 3300 microM. [Y (*)] in vivo and on affinity-purified Strep-beta in vitro was determined by EPR spectroscopy and Western analysis. In both cases, there was 0.1-0.3 Y (*) radical per beta. To determine if the substoichiometric Y (*) level was associated with apo beta or diferric beta, titrations of crude cell extracts from these growths were carried out with reduced YfaE, a 2Fe2S ferredoxin involved in cofactor maintenance and assembly. Each titration, followed by addition of O 2 to assemble the cofactor and EPR analysis to quantitate Y (*), revealed that beta is completely loaded with a diferric cluster even when its concentration in vivo is 244 microM. These titrations, furthermore, resulted in 1 Y (*) radical per beta, the highest levels reported. Whole cell Mössbauer analysis on cells induced with 0.5 mM arabinose supports high iron loading in beta. These results suggest that modulation of the level of Y (*) in vivo in E. coli is a mechanism of regulating RNR activity.

Indexed as

Blotting, WesternElectron Spin Resonance SpectroscopyElectrophoresis, Polyacrylamide GelEscherichia coliRibonucleotide ReductasesSpectroscopy, MossbauerRibonucleotide Reductases

Identifiers

PMID18314964
PMCPMC2801593
OpenAlexW2074775358

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.