Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803.

Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803. Research Abstract Details 

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Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803. Abstract Text:

,Francisco J Florencio,Marika Lindahl,

Searching for enzymes and other proteins which can be redox-regulated by dithiol/disulphide exchange is a rapidly expanding area of functional proteomics. Recently, several experimental approaches using thioredoxins have been developed for this purpose. Thioredoxins comprise a large family of redox-active enzymes capable of reducing protein disulphides to cysteines and of participating in a variety of processes, such as enzyme modulation, donation of reducing equivalents and signal transduction. In this study we screened the target proteomes of three different thioredoxins from the unicellular cyanobacterium Synechocystis sp. PCC 6803, using site-directed active-site cysteine-to-serine mutants of its m-, x- and y-type thioredoxins. The properties of a thioredoxin that determine the outcome of such analyses were found to be target-binding capacity, solubility and the presence of non-active-site cysteines. Thus, we explored how the choice of thioredoxin affects the target proteomes and we conclude that the m-type thioredoxin, TrxA, is by far the most useful for screening of disulphide proteomes. Furthermore, we improved the resolution of target proteins on non-reducing/reducing 2-DE, leading to the identification of 14 new potentially redox-regulated proteins in this organism. The presence of glycogen phosphorylase among the newly identified targets suggests that glycogen breakdown is redox-regulated in addition to glycogen synthesis.

Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803. Publishing Authors By Initials

ME ,FJ Florencio,M Lindahl,

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Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Proteomics

VOLUME: 6 Suppl 1

Page Numbers: S186-95

Journal Abbreviation: Proteomics

ISSN: 1615-9853

DAY: 24

MONTH: Apr

YEAR: 2006

Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803. Information

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LANGUAGE: eng

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Grant and Affiliation Information for Selecting thioredoxins for disulphide proteomics: Target proteomes of three thioredoxins from the cyanobacterium Synechocystis sp. PCC 6803.

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

Country: Germany

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MEDLINETA: Proteomics

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