NDLI: Identification of an essential cysteinyl residue for the structure of glutamine synthetase α from Phaseolus vulgaris

Content Provider	Springer Nature Link
Author	Estivill, Guillermo Guardado, Pilar Buser, Raymond Betti, Marco Márquez, Antonio J.
Copyright Year	2010
Abstract	We have studied the possible role, in a plant glutamine synthetase (GS), of the different cysteinyl residues present in this enzyme. For this purpose we carried out the site-directed mutagenesis of the cDNA for α-GS polypeptide from Phaseolus vulgaris in the positions corresponding to Cys-92, Cys-159, and Cys-179, followed by heterologous expression in E. coli and enzymatic characterisation of WT and mutant proteins. The results show that neither Cys-92 nor Cys-179 residues were essential for enzyme activity, but the replacement of Cys-159 by alanine or serine strongly affects the quaternary structure and function of the GS enzyme molecule, resulting in a complete loss of enzymatic activity. Other studies using sulfhydryl specific reagents such as pHMB (p-hydroxymercuribenzoate) or DTNB (5,5′-dithiobis-2-nitrobenzoate) confirmed that the profound inhibition produced is associated with an important alteration of the quaternary structure of GS, and suggest that Cys-159 might be the residue responsible for the enzyme inhibition. All these results suggest that the Cys-159 residue is essential for the enzyme structure. The results are also consistent with previous reports based on classical biochemistry studies indicating the presence of essential cysteinyl residues for the enzyme activity of higher plant GS.
Starting Page	1101
Ending Page	1111
Page Count	11
File Format	PDF
ISSN	00320935
Journal	Planta
Volume Number	231
Issue Number	5
e-ISSN	14322048
Language	English
Publisher	Springer-Verlag
Publisher Date	2010-02-21
Publisher Place	Berlin/Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Ammonium assimilation Cysteine Glutamine synthetase Quaternary structure Ecology Forestry Agriculture Plant Sciences
Content Type	Text
Resource Type	Article
Subject	Genetics Plant Science

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