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231225s2019 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erz213
|2 doi
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|a pubmed24n0989.xml
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|a (DE-627)NLM296751189
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|a (NLM)31055601
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Selles, Benjamin
|e verfasserin
|4 aut
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|a Rhodanese domain-containing sulfurtransferases
|b multifaceted proteins involved in sulfur trafficking in plants
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|c 2019
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 16.07.2020
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|a Date Revised 16.07.2020
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
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|a Sulfur is an essential element for the growth and development of plants, which synthesize cysteine and methionine from the reductive assimilation of sulfate. Besides its incorporation into proteins, cysteine is the building block for the biosynthesis of numerous sulfur-containing molecules and cofactors. The required sulfur atoms are extracted either directly from cysteine by cysteine desulfurases or indirectly after its catabolic transformation to 3-mercaptopyruvate, a substrate for sulfurtransferases (STRs). Both enzymes are transiently persulfidated in their reaction cycle, i.e. the abstracted sulfur atom is bound to a reactive cysteine residue in the form of a persulfide group. Trans-persulfidation reactions occur when sulfur atoms are transferred to nucleophilic acceptors such as glutathione, proteins, or small metabolites. STRs form a ubiquitous, multigenic protein family. They are characterized by the presence of at least one rhodanese homology domain (Rhd), which usually contains the catalytic, persulfidated cysteine. In this review, we focus on Arabidopsis STRs, presenting the sequence characteristics of all family members as well as their biochemical and structural features. The physiological functions of particular STRs in the biosynthesis of molybdenum cofactor, thio-modification of cytosolic tRNAs, arsenate tolerance, cysteine catabolism, and hydrogen sulfide formation are also discussed
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Review
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|a Cysteine
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|a hydrogen sulfide signaling
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|a persulfide group
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|a rhodanese
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|a sulfur trafficking
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|a sulfurtransferase
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|a Plant Proteins
|2 NLM
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|a Sulfur
|2 NLM
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|a 70FD1KFU70
|2 NLM
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|a Sulfurtransferases
|2 NLM
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|a EC 2.8.1.-
|2 NLM
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|a Moseler, Anna
|e verfasserin
|4 aut
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|a Rouhier, Nicolas
|e verfasserin
|4 aut
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| 700 |
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|a Couturier, Jérémy
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 70(2019), 16 vom: 19. Aug., Seite 4139-4154
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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|g volume:70
|g year:2019
|g number:16
|g day:19
|g month:08
|g pages:4139-4154
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|u http://dx.doi.org/10.1093/jxb/erz213
|3 Volltext
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|d 70
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