| pubmed-article:8132603 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8132603 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:8132603 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:8132603 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:8132603 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:8132603 | lifeskim:mentions | umls-concept:C1150528 | lld:lifeskim |
| pubmed-article:8132603 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:8132603 | pubmed:dateCreated | 1994-4-21 | lld:pubmed |
| pubmed-article:8132603 | pubmed:abstractText | EnvZ is a membrane-bound histidine kinase that functions as an osmotic sensor capable of phosphorylating the regulator protein OmpR in Escherichia coli. To characterize the site of phosphorylation biochemically, we overexpressed a 36-kDa truncated EnvZ protein (Glu-106 to Gly-450) that formed inclusion bodies in the cell. After solubilization, the inclusion body form of EnvZ was cleaved into two major fragments with molecular weights of 25,000 and 10,000. The 25-kDa fragment, EnvZc, was purified and found to exist as a dimer. N-terminal sequence analysis established that cleavage had occurred at Arg-214, indicating that EnvZc contained most of the cytoplasmic domain of EnvZ. After labeling EnvZc with [gamma-32P]ATP, the protein was proteolytically digested, and the resulting peptides were separated by reverse phase chromatography using high performance liquid chromatography. One major radioactive peptide containing greater than 90% of the recovered peptide-associated radioactivity was isolated. Amino acid analysis of this purified peptide indicated that the composition was consistent with a peptide that contained His-243. The amino acid sequence of this peptide was determined to be MAGVSHDLRTP (residues 238-248). These results indicate that His-243 is the major site of phosphorylation on EnvZ and represents the first biochemical characterization of the site of phosphorylation of a membrane histidine kinase of the two-component regulatory family of molecules in bacteria. | lld:pubmed |
| pubmed-article:8132603 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8132603 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8132603 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8132603 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8132603 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8132603 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8132603 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8132603 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8132603 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8132603 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8132603 | pubmed:author | pubmed-author:RobertsD LDL | lld:pubmed |
| pubmed-article:8132603 | pubmed:author | pubmed-author:BennettD WDW | lld:pubmed |
| pubmed-article:8132603 | pubmed:author | pubmed-author:ForstS ASA | lld:pubmed |
| pubmed-article:8132603 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8132603 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:8132603 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8132603 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8132603 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8132603 | pubmed:pagination | 8728-33 | lld:pubmed |
| pubmed-article:8132603 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8132603 | pubmed:meshHeading | pubmed-meshheading:8132603-... | lld:pubmed |
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| pubmed-article:8132603 | pubmed:meshHeading | pubmed-meshheading:8132603-... | lld:pubmed |
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| pubmed-article:8132603 | pubmed:meshHeading | pubmed-meshheading:8132603-... | lld:pubmed |
| pubmed-article:8132603 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8132603 | pubmed:articleTitle | Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli. | lld:pubmed |
| pubmed-article:8132603 | pubmed:affiliation | Department of Chemistry, University of Wisconsin-Milwaukee 53201. | lld:pubmed |
| pubmed-article:8132603 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8132603 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8132603 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:947272 | entrezgene:pubmed | pubmed-article:8132603 | lld:entrezgene |
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