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Interaction between adenylate kinase 3 and glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii.
- Source :
-
The FEBS journal [FEBS J] 2018 Jul; Vol. 285 (13), pp. 2495-2503. Date of Electronic Publication: 2018 May 16. - Publication Year :
- 2018
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Abstract
- The critical and ubiquitous enzyme adenylate kinase (ADK) catalyzes the nucleotide phosphoryl exchange reaction: 2ADP ↔ ATP + AMP. The ADK3 in the chloroplasts of the green alga Chlamydomonas reinhardtii, bears an unusual C-terminal extension that is similar to the C-terminal end of the intrinsically disordered protein CP12. In this study, we report that this enzyme, when oxidized but not when reduced, is able to interact with the chloroplast glyceraldehyde-3-phosphate dehydrogenase (GAPDH) forming a stable complex as shown by native electrophoresis and mass spectrometry. In this bienzyme complex, the activity of ADK3 is unchanged while the NADPH-dependent activity of GAPDH is significantly inhibited. Moreover ADK3, like CP12, can protect GAPDH against thermal inactivation and aggregation. The ADK3-GAPDH bienzyme complex is unable to recruit phosphoribulokinase (PRK), in contrast with the ternary complex formed between GAPDH-CP12 and PRK. The interaction between ADK3 and GAPDH might be a mechanism to regulate the crucial ATP: NADPH ratio within chloroplasts to optimize the Calvin-Benson cycle during rapid fluctuation in environmental resources.<br />Enzymes: Adenylate kinase (EC 2.7.4.3), glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.13), phosphoribulokinase (PRK, EC 2.7.1.19).<br /> (© 2018 Federation of European Biochemical Societies.)
- Subjects :
- Adenylate Kinase genetics
Algal Proteins genetics
Amino Acid Sequence
Chlamydomonas reinhardtii genetics
Chlamydomonas reinhardtii metabolism
Chloroplasts enzymology
Chloroplasts metabolism
Glyceraldehyde-3-Phosphate Dehydrogenases genetics
Immunoblotting
Multiprotein Complexes metabolism
NADP metabolism
Oxidation-Reduction
Photosynthesis
Protein Binding
Sequence Homology, Amino Acid
Tandem Mass Spectrometry
Adenylate Kinase metabolism
Algal Proteins metabolism
Chlamydomonas reinhardtii enzymology
Glyceraldehyde-3-Phosphate Dehydrogenases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1742-4658
- Volume :
- 285
- Issue :
- 13
- Database :
- MEDLINE
- Journal :
- The FEBS journal
- Publication Type :
- Academic Journal
- Accession number :
- 29727516
- Full Text :
- https://doi.org/10.1111/febs.14494