scholarly journals The Phosphate-Binding Protein of Escherichia coliIs Not Essential for Pi-Regulated Expression of thepho Regulon

2001 ◽  
Vol 183 (19) ◽  
pp. 5768-5771 ◽  
Author(s):  
Sally M. Hoffer ◽  
Jan Tommassen

ABSTRACT Disruption of pstS encoding the Pi-binding protein in Escherichia coli generally leads to the constitutive expression of thepho regulon. We demonstrate that Pi-controlled expression is restored when the activity of the Pitransporter PitA or PitB is increased. Apparently, PstS is not an essential component of the signal transduction pathway.

1992 ◽  
Vol 12 (3) ◽  
pp. 1234-1238
Author(s):  
A Lazaris-Karatzas ◽  
N Sonenberg

We present evidence that eIF-4E, the mRNA 5' cap-binding protein, cooperates with two immortalizing oncogenes, v-myc and E1A, to cause transformation of rat embryo fibroblasts. eIF-4E alone can transform rat embryo fibroblasts when selection is applied. The pattern of transformation by eIF-4E is similar to that of p21 Ras, raising the possibility that eIF-4E shares a common signal transduction pathway with p21 Ras.


Genetics ◽  
1998 ◽  
Vol 150 (4) ◽  
pp. 1349-1359 ◽  
Author(s):  
W-T Walter Lau ◽  
Ken R Schneider ◽  
Erin K O’Shea

Abstract In the yeast Saccharomyces cerevisiae, transcription of a secreted acid phosphatase, PHO5, is repressed in response to high concentrations of extracellular inorganic phosphate. To investigate the signal transduction pathway leading to transcriptional regulation of PHO5, we carried out a genetic selection for mutants that express PHO5 constitutively. We then screened for mutants whose phenotypes are also dependent on the function of PHO81, which encodes an inhibitor of the Pho80p-Pho85p cyclin/cyclin-dependent kinase complex. These mutations are therefore likely to impair upstream functions in the signaling pathway, and they define five complementation groups. Mutations were found in a gene encoding a plasma membrane ATPase (PMA1), in genes required for the in vivo function of the phosphate transport system (PHO84 and PHO86), in a gene involved in the fatty acid synthesis pathway (ACC1), and in a novel, nonessential gene (PHO23). These mutants can be classified into two groups: pho84, pho86, and pma1 are defective in high-affinity phosphate uptake, whereas acc1 and pho23 are not, indicating that the two groups of mutations cause constitutive expression of PHO5 by distinct mechanisms. Our observations suggest that these gene products affect different aspects of the signal transduction pathway for PHO5 repression.


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