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Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin.

Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Research Abstract Details 

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  • Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Abstract Text:

    alejandro mata-cabanaAlejandro Mata-Cabana,francisco j florencioFrancisco J Florencio,marika lindahlMarika Lindahl,alejandro mata-cabanaAlejandro Mata-Cabana,francisco j florencioFrancisco J Florencio,marika lindahlMarika Lindahl,

    Cysteine dithiol/disulphide exchange forms the molecular basis for regulation of a wide variety of enzymatic activities and for transduction of cellular signals. Thus, the search for proteins with reactive, accessible cysteines is expected to contribute to the unravelling of new molecular mechanisms for enzyme regulation and signal transduction. Several methods have been designed for this purpose taking advantage of the interactions between thioredoxins and their protein substrates. Thioredoxins comprise a family of redox-active enzymes, which catalyse reduction of protein disulphides and sulphenic acids. Due to the inherent practical difficulties associated with studies of membrane proteins these have been largely overlooked in the many proteomic studies of thioredoxin-interacting proteins. In the present work, we have developed a procedure to isolate membrane proteins interacting with thioredoxin by binding in situ to a monocysteinic His-tagged thioredoxin added directly to the intact membranes. Following fractionation and solubilisation of the membranes, thioredoxin target proteins were isolated by Ni-affinity chromatography and 2-DE SDS-PAGE under nonreducing/reducing conditions. Applying this method to total membranes, including thylakoid and plasma membranes, from the cyanobacterium Synechocystis sp. PCC 6803 we have identified 50 thioredoxin-interacting proteins. Among the 38 newly identified thioredoxin targets are the ATP-binding subunits of several transporters and members of the AAA-family of ATPases.

    Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Publishing Authors By Initials

    a mata-cabanaA Mata-Cabana,fj florencioFJ Florencio,m lindahlM Lindahl,a mata-cabanaA Mata-Cabana,fj florencioFJ Florencio,m lindahlM Lindahl,

    For similar abstracts research abstracts see: abstracts research

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    Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Proteomics

    VOLUME: 7

    Page Numbers: 3953-63

    Journal Abbreviation: Proteomics

    ISSN: 1615-9853

    DAY: 31

    MONTH: Nov

    YEAR: 2007

    Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Information

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    LANGUAGE: eng

    NlmUniqueID: 101092707

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    Grant and Affiliation Information for Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin.

    AFFILIATION: Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas - Universidad de Sevilla, Sevilla, Spain.

    Country: Germany

    Germany Research PublicationGermany Research Publication

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    MEDLINETA: Proteomics

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