PubMed:8132603 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":91},"obj":"Sentence"},{"id":"T2","span":{"begin":92,"end":244},"obj":"Sentence"},{"id":"T3","span":{"begin":245,"end":415},"obj":"Sentence"},{"id":"T4","span":{"begin":416,"end":551},"obj":"Sentence"},{"id":"T5","span":{"begin":552,"end":623},"obj":"Sentence"},{"id":"T6","span":{"begin":624,"end":775},"obj":"Sentence"},{"id":"T7","span":{"begin":776,"end":979},"obj":"Sentence"},{"id":"T8","span":{"begin":980,"end":1101},"obj":"Sentence"},{"id":"T9","span":{"begin":1102,"end":1231},"obj":"Sentence"},{"id":"T10","span":{"begin":1232,"end":1324},"obj":"Sentence"},{"id":"T11","span":{"begin":1325,"end":1586},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":91},"obj":"Sentence"},{"id":"T2","span":{"begin":92,"end":244},"obj":"Sentence"},{"id":"T3","span":{"begin":245,"end":415},"obj":"Sentence"},{"id":"T4","span":{"begin":416,"end":551},"obj":"Sentence"},{"id":"T5","span":{"begin":552,"end":623},"obj":"Sentence"},{"id":"T6","span":{"begin":624,"end":775},"obj":"Sentence"},{"id":"T7","span":{"begin":776,"end":979},"obj":"Sentence"},{"id":"T8","span":{"begin":980,"end":1101},"obj":"Sentence"},{"id":"T9","span":{"begin":1102,"end":1231},"obj":"Sentence"},{"id":"T10","span":{"begin":1232,"end":1324},"obj":"Sentence"},{"id":"T11","span":{"begin":1325,"end":1586},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli.\nEnvZ 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."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":74,"end":90},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":227,"end":243},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1577,"end":1585},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"562"},{"id":"A2","pred":"db_id","subj":"T2","obj":"562"},{"id":"A3","pred":"db_id","subj":"T3","obj":"2"},{"id":"A4","pred":"db_id","subj":"T3","obj":"629395"}],"text":"Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli.\nEnvZ 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."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":102,"end":110},"obj":"Body_part"},{"id":"T4","span":{"begin":748,"end":759},"obj":"Body_part"},{"id":"T5","span":{"begin":1496,"end":1504},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0005737"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A6","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A7","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"}],"text":"Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli.\nEnvZ 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."}