Evidence map›Paper›PMID 17317566›Full record

ArticleChemistry & biology2007

Identification of a potential general acid/base in the reversible phosphoryl transfer reactions catalyzed by tyrosine recombinases: Flp H305.

Katrine L Whiteson, Yu Chen, Neeraj Chopra, Amy C Raymond, Phoebe A Rice

Open access · greenAbstract read
In one paragraph

Article in Chemistry & biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
  6. Review
  7. Article
  8. Topoisomerases and site-specific recombinases: similarities in structure and mechanism.Critical reviews in biochemistry and molecular biology · 2010
    Review
  9. Article
  10. Article
  11. Article
  12. 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 1 institution in 1 country.

Katrine L WhitesonDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Yu Chen
Neeraj Chopra
Amy C Raymond
Phoebe A Rice
University of Chicago · US

Funding

Structure and Biochemistry of Recombinase-DNA ComplexesR01GM058827 · NIGMS · UNIVERSITY OF CHICAGO · PI RICE, PHOEBE A · 1999 to 2008
$2.0M
NIGMS NIH HHS GM058827NIGMS NIH HHS R01 GM058827
6 · The paper itself

Abstract

Flp provides a unique opportunity to apply the tools of chemical biology to phosphoryl transfer reactions. Flp and other tyrosine recombinases catalyze site-specific DNA rearrangements via a phosphotyrosine intermediate. Unlike most related enzymes, Flp's nucleophilic tyrosine derives from a different protomer than the remainder of its active site. Because the tyrosine can be supplied exogenously, nonnatural synthetic analogs can be used. Here we examine the catalytic role of Flp's conserved H305. DNA cleavage was studied using a peptide containing either tyrosine (pKa congruent with 10) or 3-fluoro-tyrosine (pKa congruent with 8.4). Religation was studied using DNA substrates with 3'-phospho-cresol (pKa congruent with 10) or 3'-para-nitro-phenol (pKa congruent with 7.1). In both cases, the tyrosine analog with the lower pKa specifically restored the activity of an H305 mutant. These results provide experimental evidence that this conserved histidine functions as a general acid/base catalyst in tyrosine recombinases.

Indexed as

DNA CleavageCatalysisDNA, FungalDNA NucleotidyltransferasesDNA RepairElectrophoretic Mobility Shift AssayModels, MolecularMutagenesis, Site-DirectedPhosphorylationSaccharomyces cerevisiae ProteinsTyrosineDNA, FungalDNA NucleotidyltransferasesFLP recombinaseSaccharomyces cerevisiae ProteinsTyrosine

Identifiers

PMID17317566
PMCPMC1857323
OpenAlexW2024148643

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.