Evidence map›Paper›PMID 31831819›Full record

ArticleScientific reports2019

Tuning the in vitro sensing and signaling properties of cyanobacterial PII protein by mutation of key residues.

Khaled A Selim, Michael Haffner, Björn Watzer, Karl Forchhammer

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

12 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Deciphering guanidine assimilation and riboswitch-based gene regulation in cyanobacteria for synthetic biology applications.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. ComFB, a widespread family of c-di-NMP receptor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. c-di-GMP-Dependent Regulation of Motility bybioRxiv : the preprint server for biology · 2025
    Article
  7. ComFB, a new widespread family of c-di-NMP receptor proteins.bioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

4 authors at 1 institution in 1 country.

Khaled A SelimInterfaculty Institute of Microbiology and Infection Medicine, Department of Organismic Interactions, Eberhard Karls University of Tübingen, Auf der Morgenstelle 28, 72076, Tübingen, Germany. Khaled.selim@uni-tuebingen.de.
Michael HaffnerInterfaculty Institute of Microbiology and Infection Medicine, Department of Organismic Interactions, Eberhard Karls University of Tübingen, Auf der Morgenstelle 28, 72076, Tübingen, Germany.
Björn WatzerInterfaculty Institute of Microbiology and Infection Medicine, Department of Organismic Interactions, Eberhard Karls University of Tübingen, Auf der Morgenstelle 28, 72076, Tübingen, Germany.
Karl ForchhammerInterfaculty Institute of Microbiology and Infection Medicine, Department of Organismic Interactions, Eberhard Karls University of Tübingen, Auf der Morgenstelle 28, 72076, Tübingen, Germany.
University of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PII proteins comprise an ancient superfamily of signal transduction proteins, widely distributed among all domains of life. In general, PII proteins measure and integrate the current carbon/nitrogen/energy status of the cell through interdependent binding of ATP, ADP and 2-oxogluterate. In response to effector molecule binding, PII proteins interact with various PII-receptors to tune central carbon- and nitrogen metabolism. In cyanobacteria, PII regulates, among others, the key enzyme for nitrogen-storage, N-acetyl-glutamate kinase (NAGK), and the co-activator of the global nitrogen-trascription factor NtcA, the PII-interacting protein-X (PipX). One of the remarkable PII variants from Synechococcus elongatus PCC 7942 that yielded mechanistic insights in PII-NAGK interaction, is the NAGK-superactivating variant I86N. Here we studied its interaction with PipX. Another critical residue is Lys58, forming a salt-bridge with 2-oxoglutarate in a PII-ATP-2-oxoglutarate complex. Here, we show that Lys58 of PII protein is a key residue for mediating PII interactions. The K58N mutation not only causes the loss of 2-oxogluterate binding but also strongly impairs binding of ADP, NAGK and PipX. Remarkably, the exchange of the nearby Leu56 to Lys in the K58N variant partially compensates for the loss of K58. This study demonstrates the potential of creating custom tailored PII variants to modulate metabolism.

Indexed as

Bacterial ProteinsMutation, MissensePII Nitrogen Regulatory ProteinsSignal TransductionSynechococcusAmino Acid SubstitutionBacterial ProteinsPII Nitrogen Regulatory Proteins

Identifiers

PMID31831819
PMCPMC6908673
OpenAlexW2995806068

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.