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P(II) signal transducers: novel functional and structural insights.
- K. Forchhammer
- Biology, ChemistryTrends in microbiology
- 1 February 2008
Acclimation of unicellular cyanobacteria to macronutrient deficiency: emergence of a complex network of cellular responses.
This review surveys the molecular mechanisms underlying acclimation responses to nitrogen and phosphorus deprivation, with an emphasis on non-diazotrophic freshwater cyanobacteria.
Selenocysteine: the 21st amino acid
The aim of this article is to review the events leading to the elucidation of selenocysteine as being the 21st amino acid.
Interaction network in cyanobacterial nitrogen regulation: PipX, a protein that interacts in a 2‐oxoglutarate dependent manner with PII and NtcA
PipX, a protein only present in cyanobacteria, interacts with both PII and NtcA and provides a mechanistic link between these two factors, implying that PipX may function as a prokaryotic transcriptional coactivator.
Structural basis for the regulation of NtcA-dependent transcription by proteins PipX and PII
- J. Llácer, J. Espinosa, M. A. Castells, A. Contreras, K. Forchhammer, V. Rubio
- Biology, ChemistryProceedings of the National Academy of Sciences
- 17 August 2010
The structure of active dimeric NtcA closely resembles that of the active cAMP receptor protein (CRP) closely suggests that with these proteins DNA binding, transcription activation, and allosteric regulation occur by common mechanisms, although the effectors are different.
Nitrogen starvation-induced chlorosis in Synechococcus PCC 7942. Low-level photosynthesis as a mechanism of long-term survival.
- J. Sauer, U. Schreiber, R. Schmid, U. Völker, K. Forchhammer
- Environmental Science, BiologyPlant physiology
- 1 May 2001
Long-term chlorotic cells carried out protein synthesis at a very low, but detectable level, as revealed by in vivo Methionine labeling and two-dimensional gel electrophoresis, which implies a continuous protein turnover during chlorosis.
The Synechococcus elongatus PII signal transduction protein controls arginine synthesis by complex formation with N‐acetyl‐l‐glutamate kinase
- A. Heinrich, Mani Maheswaran, U. Ruppert, K. Forchhammer
- Chemistry, BiologyMolecular microbiology
- 1 June 2004
This communication identifies, for the first time, a receptor protein for signal perception from the PII signal transduction protein in the cyanobacterium Synechococcus elongatus, subjecting the key enzyme of arginine biosynthesis to global nitrogen control.
Structural analysis of the PP2C phosphatase tPphA from Thermosynechococcus elongatus: a flexible flap subdomain controls access to the catalytic site.
Complex Formation and Catalytic Activation by the PII Signaling Protein of N-Acetyl-l-glutamate Kinase from Synechococcus elongatus Strain PCC 7942*
- Mani Maheswaran, C. Urbanke, K. Forchhammer
- Chemistry, BiologyJournal of Biological Chemistry
- 31 December 2004
The signal transduction protein PII from the cyanobacterium Synechococcus elongatus strain PCC 7942 forms a complex with the key enzyme of arginine biosynthesis, N-acetyl-l-glutamate kinase (NAGK).…
Interaction of the Membrane-bound GlnK-AmtB Complex with the Master Regulator of Nitrogen Metabolism TnrA in Bacillus subtilis*
- A. Heinrich, K. Woyda, K. Forchhammer
- Biology, ChemistryJournal of Biological Chemistry
- 17 November 2006
Immunoprecipitation and co-localization experiments identified a novel interaction between the BsGlnK-AmtB complex and the major transcription factor of nitrogen metabolism, TnrA, which may present a novel mechanism to control the global nitrogen-responsive transcription regulator TNRA in B. subtilis under certain physiological conditions.