Evidence map›Paper›PMID 16468998›Full record

ArticleMolecular microbiology2006

A new protein superfamily includes two novel 3-methyladenine DNA glycosylases from Bacillus cereus, AlkC and AlkD.

Ingrun Alseth, Torbjørn Rognes, Toril Lindbäck, Inger Solberg, Kristin Robertsen, Knut Ivan Kristiansen, Davide Mainieri, Lucy Lillehagen, Anne-Brit Kolstø, Magnar Bjørås

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

38 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Diversity and structural-functional insights of alpha-solenoid proteins.Protein science : a publication of the Protein Society · 2024
    Review
  3. Article
  4. Article
  5. Dynamic features of human mitochondrial DNA maintenance and transcription.Frontiers in cell and developmental biology · 2022
    Review
  6. Article
  7. Article
  8. Target search and recognition mechanisms of glycosylase AlkD revealed by scanning FRET-FCS and Markov state models.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. The Sole DNA Ligase inFrontiers in cellular and infection microbiology · 2018
    Article
  15. Article
  16. Article
  17. Structure of a DNA glycosylase that unhooks interstrand cross-links.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Article
  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

10 authors at 2 institutions in 1 country.

Ingrun AlsethDepartment of Molecular Biology, Institute of Medical Microbiology and Centre of Molecular Biology and Neuroscience, University of Oslo, Rikshospitalet-Radiumhospitalet HF, N-0027 Oslo, Norway.
Torbjørn Rognes
Toril Lindbäck
Inger Solberg
Kristin Robertsen
Knut Ivan Kristiansen
Davide Mainieri
Lucy Lillehagen
Anne-Brit Kolstø
Magnar Bjørås
Oslo University Hospital · NOUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Soil bacteria are heavily exposed to environmental methylating agents such as methylchloride and may have special requirements for repair of alkylation damage on DNA. We have used functional complementation of an Escherichia coli tag alkA mutant to screen for 3-methyladenine DNA glycosylase genes in genomic libraries of the soil bacterium Bacillus cereus. Three genes were recovered: alkC, alkD and alkE. The amino acid sequence of AlkE is homologous to the E. coli AlkA sequence. AlkC and AlkD represent novel proteins without sequence similarity to any protein of known function. However, iterative and indirect sequence similarity searches revealed that AlkC and AlkD are distant homologues of each other within a new protein superfamily that is ubiquitous in the prokaryotic kingdom. Homologues of AlkC and AlkD were also identified in the amoebas Entamoeba histolytica and Dictyostelium discoideum, but no other eukaryotic counterparts of the superfamily were found. The alkC and alkD genes were expressed in E. coli and the proteins were purified to homogeneity. Both proteins were found to be specific for removal of N-alkylated bases, and showed no activity on oxidized or deaminated base lesions in DNA. B. cereus AlkC and AlkD thus define novel families of alkylbase DNA glycosylases within a new protein superfamily.

Indexed as

AlkylationBacillus cereusDNA DamageDNA GlycosylasesEscherichia coliGenetic Complementation TestMultigene FamilyMutationOpen Reading FramesSequence Homology, Amino Acid3-methyladenine-DNA glycosylaseDNA-3-methyladenine glycosidase IIDNA Glycosylases

Identifiers

PMID16468998
PMCPMC1413580
OpenAlexW2104327623

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.