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rdf:type |
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lifeskim:mentions |
umls-concept:C0014834,
umls-concept:C0031727,
umls-concept:C0033684,
umls-concept:C0037083,
umls-concept:C0439851,
umls-concept:C0441655,
umls-concept:C0851285,
umls-concept:C1514562,
umls-concept:C1552596,
umls-concept:C1704675,
umls-concept:C1707723,
umls-concept:C1709061,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1947931
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pubmed:issue |
44
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pubmed:dateCreated |
2000-11-28
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pubmed:abstractText |
The PII signal transduction protein regulates the transcription of nitrogen-regulated genes by controlling the kinase and phosphatase activities of NRII. We used a cross-linking approach to study the interaction of the T-loop of the PII protein with NRII. Cross-linking of PII to NRII required ATP and 2-ketoglutarate, allosteric effectors known to control PII activity, and was not affected by the presence of excess nonspecific proteins such as bovine serum albumin. The purified cross-linked species appeared to consist mainly of PII trimers in which one of the three subunits was cross-linked to a single subunit of the NRII dimer; this complex had the phosphatase activity characteristic of the un-cross-linked PII-NRII complex, and had significant phosphatase activity in the absence of 2-ketoglutarate, suggesting that once PII was tethered to NRII the active conformation was stabilized. Studies with truncated forms of NRII indicated that the purified N-terminal "sensory" domain of NRII was not cross-linked to PII, nor was a polypeptide consisting of NRII residues 1-189. In contrast, polypeptides containing the kinase domain of the transmitter module of NRII (residues 190-349) were cross-linked to PII in an ATP- and 2-ketoglutarate-dependent reaction. These results indicate that PII controls NRII by interaction with the conserved kinase domain of the transmitter module.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorobenzenes,
http://linkedlifedata.com/resource/pubmed/chemical/Maleimides,
http://linkedlifedata.com/resource/pubmed/chemical/N-(4-azido-2,3,5,6-tetrafluorobenzyl...,
http://linkedlifedata.com/resource/pubmed/chemical/PII Nitrogen Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PIID regulatory protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase-phosphatase NTRB
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13450-61
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11063581-Bacterial Proteins,
pubmed-meshheading:11063581-Chromatography, Gel,
pubmed-meshheading:11063581-Cross-Linking Reagents,
pubmed-meshheading:11063581-Cysteine,
pubmed-meshheading:11063581-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11063581-Enzyme Activation,
pubmed-meshheading:11063581-Escherichia coli,
pubmed-meshheading:11063581-Fluorobenzenes,
pubmed-meshheading:11063581-Maleimides,
pubmed-meshheading:11063581-Mutagenesis, Site-Directed,
pubmed-meshheading:11063581-PII Nitrogen Regulatory Proteins,
pubmed-meshheading:11063581-Peptide Fragments,
pubmed-meshheading:11063581-Peptide Mapping,
pubmed-meshheading:11063581-Phosphoprotein Phosphatases,
pubmed-meshheading:11063581-Phosphorylation,
pubmed-meshheading:11063581-Protein Kinases,
pubmed-meshheading:11063581-Protein Structure, Tertiary,
pubmed-meshheading:11063581-Serine,
pubmed-meshheading:11063581-Signal Transduction
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pubmed:year |
2000
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pubmed:articleTitle |
The Escherichia coli PII signal transduction protein regulates the activities of the two-component system transmitter protein NRII by direct interaction with the kinase domain of the transmitter module.
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pubmed:affiliation |
Department of Biological Chemistry and Human Genetics Training Program, University of Michigan Medical School, Ann Arbor, Michigan 48109-0606, USA.
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pubmed:publicationType |
Journal Article
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