The extended N-terminal region of SphS is required for detection of external phosphate levels in Synechocystis sp. PCC 6803

A novel 47 amino acid extension at the N-terminus of the SphS histidine kinase has been identified in the cyanobacterium Synechocystis sp. PCC 6803. Here, we demonstrate this region is required for activation of the SphS–SphR phosphate-sensing two-component system under phosphate-limiting conditions...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2009-01, Vol.378 (3), p.383-388
Main Authors: Burut-Archanai, Surachet, Incharoensakdi, Aran, Eaton-Rye, Julian J.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - genetics
Bacterial Proteins - physiology
Biological Transport
Cyanophyta
Molecular Sequence Data
N-terminus of SphS
Phosphate detection
Phosphates - metabolism
Phosphotransferases - genetics
Phosphotransferases - physiology
Protein Structure, Tertiary
Pst system
Regulon
Sequence Deletion
SphS transmembrane domain
SphU
Synechocystis
Synechocystis - genetics
Synechocystis - metabolism
Synechocystis sp. PCC 6803
Transcription Factors - genetics
Transcription Factors - physiology
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Summary:A novel 47 amino acid extension at the N-terminus of the SphS histidine kinase has been identified in the cyanobacterium Synechocystis sp. PCC 6803. Here, we demonstrate this region is required for activation of the SphS–SphR phosphate-sensing two-component system under phosphate-limiting conditions and mutants lacking this extension do not show constitutive alkaline phosphatase activity when the negative regulator SphU is inactivated. We have also identified a putative membrane-associated domain within this region involved in control of the Pho regulon. In addition, there are two high-affinity ABC-type phosphate uptake systems in this organism. Our results demonstrate that the Pst1 system, but not the Pst2 system, is required for suppression of the Pho regulon under phosphate-sufficient conditions. Deletion of the pst1 operon and disruption of the membrane-spanning domain may both target the same control mechanism since constitutive alkaline phosphatase activity is similar in the double and single mutants.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2008.11.012