Results 61 to 70 of about 4,364,730 (221)

Regulatory Connections Between the Cyanobacterial Factor PipX and the Ribosome Assembly GTPase EngA

open access: yesFrontiers in Microbiology, 2021
Cyanobacteria, phototrophic organisms performing oxygenic photosynthesis, must adapt their metabolic processes to important environmental challenges, like those imposed by the succession of days and nights.
Carmen Jerez   +6 more
doaj   +1 more source

PII Overexpression in Lotus japonicus Affects Nodule Activity in Permissive Low-Nitrogen Conditions and Increases Nodule Numbers in High Nitrogen Treated Plants

open access: yesMolecular Plant-Microbe Interactions, 2015
We report here the first characterization of a GLNB1 gene coding for the PII protein in leguminous plants. The main purpose of this work was the investigation of the possible roles played by this multifunctional protein in nodulation pathways.
Enrica D’Apuzzo   +9 more
doaj   +1 more source

Distinctive Features of PipX, a Unique Signaling Protein of Cyanobacteria

open access: yesLife, 2020
PipX is a unique cyanobacterial protein identified by its ability to bind to PII and NtcA, two key regulators involved in the integration of signals of the nitrogen/carbon and energy status, with a tremendous impact on nitrogen assimilation and gene ...
Jose I. Labella   +4 more
doaj   +1 more source

Antagonism of PII signalling by the AmtB protein of Escherichia coli [PDF]

open access: yesMolecular Microbiology, 2003
Summary Escherichia coli AmtB is a member of the MEP/Amt family of ammonia transporters found in archaea, eubacteria, fungi, plants and animals. In prokaryotes, AmtB homologues are co‐transcribed with a PII paralogue, GlnK, in response to nitrogen limitation. Here, we show that AmtB antagonizes PII signalling through NRII and that co‐expression of GlnK
Blauwkamp, Timothy A.   +1 more
openaire   +3 more sources

Association and dissociation of the GlnK-AmtB complex in response to cellular nitrogen status can occur in the absence of GlnK post-translational modification

open access: yesFrontiers in Microbiology, 2014
PII proteins are pivotal players in the control of nitrogen metabolism in bacteria and archaea, and are also found in the plastids of plants. PII proteins control the activities of a diverse range of enzymes, transcription factors and membrane transport ...
Mike eMerrick   +2 more
doaj   +1 more source

Interaction of N-Acetylglutamate Kinase with a PII-Like Protein in Rice [PDF]

open access: yesPlant and Cell Physiology, 2004
PII protein in bacteria is a sensor for 2-oxoglutarate and a transmitter for glutamine signaling. We identified an OsGlnB gene that encoded a bacterial PII-like protein in rice. Yeast two-hybrid analysis showed that an OsGlnB gene product interacted with N-acetylglutamate kinase 1 (OsNAGK1) and PII-like protein (OsGlnB) itself in rice. In cyanobacteria,
Kenjiro, Sugiyama   +4 more
openaire   +2 more sources

Expanding the cyanobacterial nitrogen regulatory network: The GntR-like regulator PlmA interacts with the PII-PipX complex

open access: yesFrontiers in Microbiology, 2016
Cyanobacteria, phototrophic organisms that perform oxygenic photosynthesis, perceive nitrogen status by sensing 2-oxoglutarate levels. PII, a widespread signaling protein, senses and transduces nitrogen and energy status to target proteins, regulating ...
Jose Ignacio Labella   +7 more
doaj   +1 more source

Direct Calorimetric Determination of a Complete Polyproline II (pII) Propensity Scale Reveals PII Enhancement in Intrinsically Disordered Proteins [PDF]

open access: yesBiophysical Journal, 2011
Circular dichroism spectropolarimetry experiments and other studies have suggested that the denatured states of polypeptides may comprise a smaller conformational space than previously thought, and that the polyproline II (PII) helix is one of the conformations that is highly populated in the denatured state.
Elam, William A.   +2 more
openaire   +1 more source

A PII-like protein in Arabidopsis : Putative role in nitrogen sensing [PDF]

open access: yesProceedings of the National Academy of Sciences, 1998
PII is a protein allosteric effector in Escherichia coli and other bacteria that indirectly regulates glutamine synthetase at the transcriptional and post-translational levels in response to nitrogen availability.
M H, Hsieh   +3 more
openaire   +2 more sources

pii-codex: a Python library for PII detection, categorization, and severity assessment [PDF]

open access: yes, 2022
A research python package for detecting, categorizing, and assessing the severity of personal identifiable information (PII)If you use this software, please cite it as ...
Rosado, Eidan J., Eidan J. Rosado
core   +1 more source

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