title: The intriguing CP12-like tail of adenylate kinase 3 from Chlamydomonas reinhardtii.
abstract: Adenylate kinases (ADK) are key enzymes that maintain the energetic balance in cellular compartments by catalyzing the reaction: AMP + ATP↔2 ADP. Here, we analyzed the chloroplast ADK 3 from the green alga, Chlamydomonas reinhardtii for the first time. This enzyme bears a C-terminal extension that is highly similar to the C-terminal end of the intrinsically disordered protein CP12 that plays a major role in the redox regulation of key enzymes of the Calvin-Benson cycle like glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase. The only other known example of a CP12-like extension is found in the GapB isoform of GAPDH, where it is responsible for the autonomous redox regulation of the higher plant A2 B2 GAPDH. In this study, we show that the CP12-like tail is not involved in the redox regulation of ADK 3, but contributes greatly to its stability, and is essential for the post-translational modification of the Cys221 residue by glutathione. This report highlights the fact that the C-terminal part of the CP12 protein can act as a moonlighting, intrinsically disordered module conferring additional capabilities to the proteins to which it is added.
  
  
  
  Adenylate kinase (ADK, EC 2.7.4.3) and glyceraldehyde 3-phosphate dehydrogenase (GAPDH, EC 1.2.1.13).
authors.affiliation: Aix Marseille Univ, CNRS, BIP, UMR 7281, IMM, Marseille Cedex 20, France.
authors.forename: Gabriel
authors.initials: G
authors.lastname: Thieulin-Pardo
authors.affiliation: Aix Marseille Univ, CNRS, BIP, UMR 7281, IMM, Marseille Cedex 20, France.
authors.forename: Antoine
authors.initials: A
authors.lastname: Schramm
authors.affiliation: Plate-forme Protéomique, Marseille Protéomique (MaP), Institut de Microbiologie de la Méditerranée, CNRS, FR 3479, Marseille Cedex 20, France.
authors.forename: Sabrina
authors.initials: S
authors.lastname: Lignon
authors.affiliation: Plate-forme Protéomique, Marseille Protéomique (MaP), Institut de Microbiologie de la Méditerranée, CNRS, FR 3479, Marseille Cedex 20, France.
authors.forename: Régine
authors.initials: R
authors.lastname: Lebrun
authors.affiliation: Aix Marseille Univ, CNRS, BIP, UMR 7281, IMM, Marseille Cedex 20, France.
authors.forename: Mila
authors.initials: M
authors.lastname: Kojadinovic
authors.affiliation: Aix Marseille Univ, CNRS, BIP, UMR 7281, IMM, Marseille Cedex 20, France. bmeunier@imm.cnrs.fr.
authors.forename: Brigitte
authors.initials: B
authors.lastname: Gontero
mesh_terms: D000263:Adenylate Kinase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020418:Algal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D016825:Chlamydomonas reinhardtii / Q000201:enzymology* / Q000235:genetics; D060365:Chloroplast Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002942:Circular Dichroism; D003545:Cysteine / Q000737:chemistry; D004795:Enzyme Stability; D005978:Glutathione / Q000737:chemistry / Q000378:metabolism; D064267:Intrinsically Disordered Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
chemical_list: D020418:Algal Proteins; D060365:Chloroplast Proteins; D064267:Intrinsically Disordered Proteins; D007527:Isoenzymes; D011994:Recombinant Proteins; D000263:Adenylate Kinase; D005978:Glutathione; D003545:Cysteine
keywords: adenylate kinase redox regulation; glutathione; intrinsically disordered proteins; metabolism