| pubmed-article:8226621 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C0031603 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C1442161 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C0002085 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C0029073 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C0206522 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C0449851 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C0559956 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:8226621 | lifeskim:mentions | umls-concept:C2827421 | lld:lifeskim |
| pubmed-article:8226621 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:8226621 | pubmed:dateCreated | 1993-12-2 | lld:pubmed |
| pubmed-article:8226621 | pubmed:abstractText | The phosphate regulon is negatively regulated by the PstSCAB transporter and PhoU protein by a mechanism that may involve protein-protein interaction(s) between them and the Pi sensor protein, PhoR. In order to study such presumed interaction(s), mutants with defined deletions of the pstSCAB-phoU operon were made. This was done by construction of M13 recombinant phage carrying these mutations and by recombination of them onto the chromosome by using a rep host (which cannot replicate M13) for allele replacement. These mutants were used to show that delta (pstSCAB-phoU) and delta (pstB-phoU) mutations abolished Pi uptake by the PstSCAB transporter, as expected, and that delta phoU mutations had no effect on uptake. Unexpectedly, delta phoU mutations had a severe growth defect, and this growth defect was (largely) alleviated by a compensatory mutation in the pstSCAB genes or in the phoBR operon, whose gene products positively regulate expression of the pstSCAB-phoU operon. Because delta phoU mutants that synthesize a functional PstSCAB transporter constitutively grew extremely poorly, the PhoU protein must have a new role, in addition to its role as a negative regulator. A role for the PhoU protein in intracellular Pi metabolism is proposed. Further, our results contradict those of M. Muda, N. N. Rao, and A. Torriani (J. Bacteriol. 174:8057-8064, 1992), who reported that the PhoU protein was required for Pi uptake. | lld:pubmed |
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| pubmed-article:8226621 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8226621 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8226621 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8226621 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8226621 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:8226621 | pubmed:author | pubmed-author:WannerB LBL | lld:pubmed |
| pubmed-article:8226621 | pubmed:author | pubmed-author:SteedP MPM | lld:pubmed |
| pubmed-article:8226621 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8226621 | pubmed:volume | 175 | lld:pubmed |
| pubmed-article:8226621 | pubmed:geneSymbol | phoU | lld:pubmed |
| pubmed-article:8226621 | pubmed:geneSymbol | pstSCAB | lld:pubmed |
| pubmed-article:8226621 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8226621 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8226621 | pubmed:pagination | 6797-809 | lld:pubmed |
| pubmed-article:8226621 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8226621 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8226621 | pubmed:articleTitle | Use of the rep technique for allele replacement to construct mutants with deletions of the pstSCAB-phoU operon: evidence of a new role for the PhoU protein in the phosphate regulon. | lld:pubmed |
| pubmed-article:8226621 | pubmed:affiliation | Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907. | lld:pubmed |
| pubmed-article:8226621 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8226621 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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