Analysis of phosphorylation-dependent protein-protein interactions using a bacterial two-hybrid system.

Analysis of phosphorylation-dependent protein-protein interactions using a bacterial two-hybrid system. Research Abstract Details 

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Analysis of phosphorylation-dependent protein-protein interactions using a bacterial two-hybrid system. Abstract Text:

Phosphorylation-dependent protein-protein interactions provide the foundation for a multitude of intracellular signal transduction pathways. One of the goals of signal transduction research is to more precisely understand the nature of these phosphorylation-dependent interactions. Here, we describe a bacterial two-hybrid assay that allows for the rapid, efficient analysis of phosphorylation-dependent protein-protein interactions. In this system, the interacting protein domains are provided as fusion proteins in Escherichia coli. cells that contain a eukaryotic kinase. Specific phosphorylation of one of the fused protein domains results in a protein-protein interaction that can be detected as a change in the expression of a reporter gene. We also describe how this system can be modified to permit the use of cDNA libraries to identify either novel binding partners for a phosphorylated substrate or novel kinases that can induce a specific protein-protein interaction.

Analysis of phosphorylation-dependent protein-protein interactions using a bacterial two-hybrid system. Publishing Authors By Initials

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Analysis of phosphorylation-dependent protein-protein interactions using a bacterial two-hybrid system. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Science's STKE : signal transduction knowledge env

VOLUME: 2002

Page Numbers: PL11

Journal Abbreviation: Sci. STKE

ISSN: 1525-8882

DAY: 23

MONTH: 07

YEAR: 2002

Analysis of phosphorylation-dependent protein-protein interactions using a bacterial two-hybrid system. Information

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LANGUAGE: eng

NlmUniqueID: 100964423

Analysis of phosphorylation-dependent protein-protein interactions using a bacterial two-hybrid system. Keywords Mesh Terms:

KEYWORDS: beta-Lactamases

MESH TERMS: biosynthesis

Chemical & Substance for Abstract: Analysis of phosphorylation-dependent protein-protein interactions using a bacterial two-hybrid system. Information

Substance Name: beta-Lactamases

Registry Number: EC 3.5.2.6

Grant and Affiliation Information for Analysis of phosphorylation-dependent protein-protein interactions using a bacterial two-hybrid system.

AFFILIATION: Program in Biological and Biomedical Sciences, Division of Medical Sciences, Harvard Medical School, and Division of Neuroscience, Children's Hospital, Boston, MA 02115, USA.

Country: United States

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MEDLINETA: Sci STKE

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