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rdf:type |
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lifeskim:mentions |
umls-concept:C0008551,
umls-concept:C0014834,
umls-concept:C0033684,
umls-concept:C0037293,
umls-concept:C0181496,
umls-concept:C0596448,
umls-concept:C1150528,
umls-concept:C1167322,
umls-concept:C1511625,
umls-concept:C1522485,
umls-concept:C1522492,
umls-concept:C2752508
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pubmed:issue |
2
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pubmed:dateCreated |
1997-2-21
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pubmed:abstractText |
EnvZ is a transmembrane osmosensor which regulates the phosphorylation of OmpR, a transcription factor for ompF and ompC genes which encode the major outer membrane porin proteins, OmpF and OmpC in Escherichia coli. Autophosphorylation of EnvZ occurs through a transphosphorylation reaction between two EnvZ molecules. To elucidate the molecular mechanism of signal transduction by EnvZ, we examined the dimer formation of the EnvZ cytoplasmic domain [EnvZ(C)]. For this purpose, we developed a method to determine the complex formation between the purified EnvZ(C) and the purified His6-EnvZ(C) by means of Ni-6xhistidine tag affinity chromatography. When the mixture of EnvZ(C) and His6-EnvZ(C) was applied to Ni-NTA resin, both His6-EnvZ(C) and EnvZ(C) were bound to the resin, indicating that EnvZ can form an oligomer without the periplasmic and transmembrane domains. Binding experiments using the Ni-NTA resin revealed that EnvZ(C) forms a dimer with the Ka value for dimerization being approximately 10(5) M(-1) in the equilibrium state.
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pubmed:grant |
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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 Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Nickel,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrilotriacetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Organometallic Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Resins, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/envZ protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/nickel nitrilotriacetic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
400
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
238-42
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9001405-Bacterial Outer Membrane Proteins,
pubmed-meshheading:9001405-Chromatography, Affinity,
pubmed-meshheading:9001405-Cytoplasm,
pubmed-meshheading:9001405-Escherichia coli,
pubmed-meshheading:9001405-Escherichia coli Proteins,
pubmed-meshheading:9001405-Gene Expression,
pubmed-meshheading:9001405-Histidine,
pubmed-meshheading:9001405-Multienzyme Complexes,
pubmed-meshheading:9001405-Nickel,
pubmed-meshheading:9001405-Nitrilotriacetic Acid,
pubmed-meshheading:9001405-Organometallic Compounds,
pubmed-meshheading:9001405-Recombinant Fusion Proteins,
pubmed-meshheading:9001405-Resins, Plant
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pubmed:year |
1997
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pubmed:articleTitle |
Demonstration of dimer formation of the cytoplasmic domain of a transmembrane osmosensor protein, EnvZ, of Escherichia coli using Ni-histidine tag affinity chromatography.
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pubmed:affiliation |
Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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