Chloroplast Glyceraldehyde-3-phosphate Dehydrogenase Contains a Single Disulfide Bond Located in the C-terminal Extension to the B Subunit

Mass mapping analysis based on cyanylation and CN-induced cleavage indicates that the two cysteine residues in the C-terminal extension of the B subunit of the light-activated pea leaf chloroplast glyceraldehyde-3-phosphate dehydrogenase form a disulfide bond. No evidence was found for a disulfide b...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-09, Vol.276 (38), p.35247-35252
Main Authors: Qi, Jianfeng, Isupov, Michail N., Littlechild, Jennifer A., Anderson, Louise E.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Chloroplasts - enzymology
Chromatography, High Pressure Liquid
Disulfides - chemistry
Glyceraldehyde-3-Phosphate Dehydrogenases - chemistry
Glyceraldehyde-3-Phosphate Dehydrogenases - isolation & purification
Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism
Molecular Sequence Data
Oxidation-Reduction
Pisum sativum
Protein Conformation
Sequence Homology, Amino Acid
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Summary:Mass mapping analysis based on cyanylation and CN-induced cleavage indicates that the two cysteine residues in the C-terminal extension of the B subunit of the light-activated pea leaf chloroplast glyceraldehyde-3-phosphate dehydrogenase form a disulfide bond. No evidence was found for a disulfide bond in the A subunit, nor was there any indication of a second disulfide bond in the B subunit. The availability of the structure of the extended glyceraldehyde-3-phosphate dehydrogenase from the archaeonSulfolobus solfataricus allows modeling of the B subunit. As modeled, the two cysteine residues in the extension are positioned to form an interdomain disulfide cross-link.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M103855200