Evidence map›Paper›PMID 15716449›Full record

ArticleJournal of bacteriology2005

Structure of the nucleotide complex of PyrR, the pyr attenuation protein from Bacillus caldolyticus, suggests dual regulation by pyrimidine and purine nucleotides.

Preethi Chander, Kari M Halbig, Jamie K Miller, Christopher J Fields, Heather K S Bonner, Gail K Grabner, Robert L Switzer, Janet L Smith

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Intermolecular Communication inFrontiers in molecular biosciences · 2020
    Review
  2. Review
  3. Regulation of Bacterial Gene Expression by Transcription Attenuation.Microbiology and molecular biology reviews : MMBR · 2019
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Expression, purification and preliminary X-ray diffraction studies of the transcriptional factor PyrR from Bacillus halodurans.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. 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

8 authors at 2 institutions in 1 country.

Preethi ChanderDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana, USA.
Kari M Halbig
Jamie K Miller
Christopher J Fields
Heather K S Bonner
Gail K Grabner
Robert L Switzer
Janet L Smith
University of Illinois Urbana-Champaign · USPurdue University West Lafayette · US

Funding

STRUCTURE AND FUNCTION OF A PURINE BIOSYNTHETIC ENZYMER01DK042303 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 1990 to 2024
$6.6M
GLUTAMINE AMIDOTRANSFERASES AND PARTNER ENZYMESR37DK042303 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 1998 to 2007
$2.4M
NOVEL CONTROL MECHANISMS IN ENDOSPORE FORMATIONR01GM047112 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SWITZER, ROBERT L · 1991 to 2006
$2.0M
NIDDK NIH HHS DK42303NIDDK NIH HHS R01 DK042303NIDDK NIH HHS R37 DK042303NIGMS NIH HHS GM47112NIGMS NIH HHS R01 GM047112
6 · The paper itself

Abstract

PyrR is a protein that regulates the expression of genes and operons of pyrimidine nucleotide biosynthesis (pyr genes) in many bacteria. PyrR acts by binding to specific sequences on pyr mRNA and causing transcriptional attenuation when intracellular levels of uridine nucleotides are elevated. PyrR from Bacillus subtilis has been purified and extensively studied. In this work, we describe the purification to homogeneity and characterization of recombinant PyrR from the thermophile Bacillus caldolyticus and the crystal structures of unliganded PyrR and a PyrR-nucleotide complex. The B. caldolyticus pyrR gene was previously shown to restore normal regulation of the B. subtilis pyr operon in a pyrR deletion mutant. Like B. subtilis PyrR, B. caldolyticus PyrR catalyzes the uracil phosphoribosyltransferase reaction but with maximal activity at 60 degrees C. Crystal structures of B. caldolyticus PyrR reveal a dimer similar to the B. subtilis PyrR dimer and, for the first time, binding sites for nucleotides. UMP and GMP, accompanied by Mg2+, bind specifically to PyrR active sites. Nucleotide binding to PyrR is similar to other phosphoribosyltransferases, but Mg2+ binding differs. GMP binding was unexpected. The protein bound specific sequences of pyr RNA 100 to 1,000 times more tightly than B. subtilis PyrR, depending on the RNA tested and the assay method; uridine nucleotides enhanced RNA binding, but guanosine nucleotides antagonized it. The new findings of specific GMP binding and its antagonism of RNA binding suggest cross-regulation of the pyr operon by purines.

Indexed as

BacillusBacterial ProteinsCations, DivalentGene Expression Regulation, BacterialModels, MolecularMolecular StructurePentosyltransferasesProtein BindingProtein ConformationProtein Structure, QuaternaryPurine NucleotidesPyrimidine NucleotidesRecombinant ProteinsRepressor ProteinsRNABacterial ProteinsCations, DivalentPentosyltransferasesPurine NucleotidesPyrimidine NucleotidesPyrR protein, bacteriaRecombinant ProteinsRepressor ProteinsRNA

Identifiers

PMID15716449
PMCPMC1064020
OpenAlexW2011877182

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.