| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-91 |
Sentence |
denotes |
Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli. |
| T1 |
0-91 |
Sentence |
denotes |
Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli. |
| T2 |
92-244 |
Sentence |
denotes |
EnvZ is a membrane-bound histidine kinase that functions as an osmotic sensor capable of phosphorylating the regulator protein OmpR in Escherichia coli. |
| T2 |
92-244 |
Sentence |
denotes |
EnvZ is a membrane-bound histidine kinase that functions as an osmotic sensor capable of phosphorylating the regulator protein OmpR in Escherichia coli. |
| T3 |
245-415 |
Sentence |
denotes |
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. |
| T3 |
245-415 |
Sentence |
denotes |
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. |
| T4 |
416-551 |
Sentence |
denotes |
After solubilization, the inclusion body form of EnvZ was cleaved into two major fragments with molecular weights of 25,000 and 10,000. |
| T4 |
416-551 |
Sentence |
denotes |
After solubilization, the inclusion body form of EnvZ was cleaved into two major fragments with molecular weights of 25,000 and 10,000. |
| T5 |
552-623 |
Sentence |
denotes |
The 25-kDa fragment, EnvZc, was purified and found to exist as a dimer. |
| T5 |
552-623 |
Sentence |
denotes |
The 25-kDa fragment, EnvZc, was purified and found to exist as a dimer. |
| T6 |
624-775 |
Sentence |
denotes |
N-terminal sequence analysis established that cleavage had occurred at Arg-214, indicating that EnvZc contained most of the cytoplasmic domain of EnvZ. |
| T6 |
624-775 |
Sentence |
denotes |
N-terminal sequence analysis established that cleavage had occurred at Arg-214, indicating that EnvZc contained most of the cytoplasmic domain of EnvZ. |
| T7 |
776-979 |
Sentence |
denotes |
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. |
| T7 |
776-979 |
Sentence |
denotes |
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. |
| T8 |
980-1101 |
Sentence |
denotes |
One major radioactive peptide containing greater than 90% of the recovered peptide-associated radioactivity was isolated. |
| T8 |
980-1101 |
Sentence |
denotes |
One major radioactive peptide containing greater than 90% of the recovered peptide-associated radioactivity was isolated. |
| T9 |
1102-1231 |
Sentence |
denotes |
Amino acid analysis of this purified peptide indicated that the composition was consistent with a peptide that contained His-243. |
| T9 |
1102-1231 |
Sentence |
denotes |
Amino acid analysis of this purified peptide indicated that the composition was consistent with a peptide that contained His-243. |
| T10 |
1232-1324 |
Sentence |
denotes |
The amino acid sequence of this peptide was determined to be MAGVSHDLRTP (residues 238-248). |
| T10 |
1232-1324 |
Sentence |
denotes |
The amino acid sequence of this peptide was determined to be MAGVSHDLRTP (residues 238-248). |
| T11 |
1325-1586 |
Sentence |
denotes |
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. |
| T11 |
1325-1586 |
Sentence |
denotes |
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. |