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Interaction between adenylate kinase 3 and glyceraldehyde‐3‐phosphate dehydrogenase from Chlamydomonas reinhardtii
Author(s) -
Zhang Yizhi,
Launay Hélène,
Liu Fan,
Lebrun Régine,
Gontero Brigitte
Publication year - 2018
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14494
Subject(s) - chlamydomonas reinhardtii , glyceraldehyde 3 phosphate dehydrogenase , adenylate kinase , dehydrogenase , biochemistry , chloroplast , chemistry , ternary complex , enzyme , biology , gene , mutant
The critical and ubiquitous enzyme adenylate kinase ( ADK ) catalyzes the nucleotide phosphoryl exchange reaction: 2 ADP ↔ ATP + AMP . The ADK 3 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 CP 12. 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 ADK 3 is unchanged while the NADPH ‐dependent activity of GAPDH is significantly inhibited. Moreover ADK 3, like CP 12, can protect GAPDH against thermal inactivation and aggregation. The ADK 3‐ GAPDH bienzyme complex is unable to recruit phosphoribulokinase ( PRK ), in contrast with the ternary complex formed between GAPDH ‐ CP 12 and PRK . The interaction between ADK 3 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. 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 ).