Evidence map›Paper›PMID 10850980›Full record

ArticleJournal of bacteriology2000

Purification and characterization of Sa-lrp, a DNA-binding protein from the extreme thermoacidophilic archaeon Sulfolobus acidocaldarius homologous to the bacterial global transcriptional regulator Lrp.

J Enoru-Eta, D Gigot, T L Thia-Toong, N Glansdorff, D Charlier

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

20 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. YtrAFrontiers in microbiology · 2019
    Article
  4. Article
  5. Article
  6. Article
  7. Host and viral transcriptional regulators in Sulfolobus: an overview.Extremophiles : life under extreme conditions · 2013
    Review
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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 3 institutions in 1 country.

J Enoru-EtaErfelijkheidsleer en Microbiologie, Vrije Universiteit Brussel, and Department of Microbiology, The Flanders Interuniversity Institute for Biotechnology, Université Libre de Bruxelles, Brussels, Belgium.
D Gigot
T L Thia-Toong
N Glansdorff
D Charlier
Vlaams Instituut voor Biotechnologie · BEVrije Universiteit Brussel · BEUniversité Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Archaea, constituting the third primary domain of life, harbor a basal transcription apparatus of the eukaryotic type, whereas curiously, a large fraction of the potential transcription regulation factors appear to be of the bacterial type. To date, little information is available on these predicted regulators and on the intriguing interplay that necessarily has to occur with the transcription machinery. Here, we focus on Sa-lrp of the extremely thermoacidophilic crenarchaeote Sulfolobus acidocaldarius, encoding an archaeal homologue of the Escherichia coli leucine-responsive regulatory protein Lrp, a global transcriptional regulator and genome organizer. Sa-lrp was shown to produce a monocistronic mRNA that was more abundant in the stationary-growth phase and produced in smaller amounts in complex medium, this down regulation being leucine independent. We report on Sa-Lrp protein purification from S. acidocaldarius and from recombinant E. coli, both identified by N-terminal amino acid sequence determination. Recombinant Sa-Lrp was shown to be homotetrameric and to bind to its own control region; this binding proved to be leucine independent and was stimulated at high temperatures. Interference binding experiments suggested an important role for minor groove recognition in the Sa-Lrp-DNA complex formation, and mutant analysis indicated the importance for DNA binding of the potential helix-turn-helix motif present at the N terminus of Sa-Lrp. The DNA-binding capacity of purified Sa-Lrp was found to be more resistant to irreversible heat inactivation in the presence of L-leucine, suggesting a potential physiological role of the amino acid as a cofactor.

Indexed as

Amino Acid SubstitutionArchaeal ProteinsBase SequenceDeoxyribonuclease IDNADNA, ArchaealDNA-Binding ProteinsDNA FootprintingEscherichia coliEscherichia coli ProteinsGene ExpressionGenesHelix-Loop-Helix MotifsLeucine-Responsive Regulatory ProteinLigandsMolecular Sequence DataArchaeal ProteinsDeoxyribonuclease IDNADNA, ArchaealDNA-Binding ProteinsEscherichia coli ProteinsLeucine-Responsive Regulatory ProteinLigandsLrp protein, E coliRecombinant Fusion ProteinsRNA, ArchaealRNA, MessengerTranscription Factors

Identifiers

PMID10850980
PMCPMC94536
OpenAlexW2120072337

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.