ArticleJournal of bacteriology2005
PhoR1-PhoP1, a third two-component system of the family PhoRP from Myxococcus xanthus: role in development.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
The trial behind it
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Who cites it
3 citing papers in PubMed.
- Myxococcus xanthus Pph2 is a manganese-dependent protein phosphatase involved in energy metabolism.The Journal of biological chemistry · 2009Article
- Phosphate acquisition components of the Myxococcus xanthus Pho regulon are regulated by both phosphate availability and development.Journal of bacteriology · 2008Article
- Differential expression of the three multicopper oxidases from Myxococcus xanthus.Journal of bacteriology · 2007Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pair PhoR1-PhoP1 is the third two-component system of the family PhoRP reported in M. xanthus. PhoR1 is a histidine kinase anchored to the membrane through a transmembrane domain located in the amino-terminal portion of the protein. As a result, 93% of the protein is located in the cytoplasm. This topology is unusual in the PhoR-type histidine kinases. PhoP1 is a response regulator with a helix-loop-helix motif typical of the DNA-binding proteins. Although the operon phoPR1 is expressed during vegetative growth, it peaks during development. The expression levels of this operon are higher in phosphate-containing media than in those in which the nutrient is absent. A deletion mutant in this system exhibits a delay in aggregation and the formation of fruiting bodies larger than those of the wild-type strain. The expression of the operon is autoregulated. This system is also partially responsible for the expression of Mg-independent acid and neutral phosphatases, but it is not required for the expression of alkaline phosphatases.
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