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Inter-species variation in the oligomeric states of the higher plant Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase.

Abstract

In darkened leaves the Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK) form a regulatory multi-enzyme complex with the small chloroplast protein CP12. GAPDH also forms a high molecular weight regulatory mono-enzyme complex. Given that there are different reports as to the number and subunit composition of these complexes and that enzyme regulatory mechanisms are known to vary between species, it was reasoned that protein-protein interactions may also vary between species. Here, this variation is investigated. This study shows that two different tetramers of GAPDH (an A2B2 heterotetramer and an A4 homotetramer) have the capacity to form part of the PRK/GAPDH/CP12 complex. The role of the PRK/GAPDH/CP12 complex is not simply to regulate the 'non-regulatory' A4 GAPDH tetramer. This study also demonstrates that the abundance and nature of PRK/GAPDH/CP12 interactions are not equal in all species and that whilst NAD enhances complex formation in some species, this is not sufficient for complex formation in others. Furthermore, it is shown that the GAPDH mono-enzyme complex is more abundant as a 2(A2B2) complex, rather than the larger 4(A2B2) complex. This smaller complex is sensitive to cellular metabolites indicating that it is an important regulatory isoform of GAPDH. This comparative study has highlighted considerable heterogeneity in PRK and GAPDH protein interactions between closely related species and the possible underlying physiological basis for this is discussed.

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  • Authors+Show Affiliations

    ,

    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK. T.P.Howard@exeter.ac.uk

    ,

    Source

    Journal of experimental botany 62:11 2011 Jul pg 3799-805

    MeSH

    Chloroplasts
    Glyceraldehyde-3-Phosphate Dehydrogenases
    NAD
    Phosphotransferases (Alcohol Group Acceptor)
    Photosynthesis
    Plant Proteins
    Plants
    Protein Isoforms
    Species Specificity

    Pub Type(s)

    Comparative Study
    Journal Article
    Research Support, Non-U.S. Gov't

    Language

    eng

    PubMed ID

    21498632

    Citation

    Howard, Thomas P., et al. "Inter-species Variation in the Oligomeric States of the Higher Plant Calvin Cycle Enzymes Glyceraldehyde-3-phosphate Dehydrogenase and Phosphoribulokinase." Journal of Experimental Botany, vol. 62, no. 11, 2011, pp. 3799-805.
    Howard TP, Lloyd JC, Raines CA. Inter-species variation in the oligomeric states of the higher plant Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase. J Exp Bot. 2011;62(11):3799-805.
    Howard, T. P., Lloyd, J. C., & Raines, C. A. (2011). Inter-species variation in the oligomeric states of the higher plant Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase. Journal of Experimental Botany, 62(11), pp. 3799-805. doi:10.1093/jxb/err057.
    Howard TP, Lloyd JC, Raines CA. Inter-species Variation in the Oligomeric States of the Higher Plant Calvin Cycle Enzymes Glyceraldehyde-3-phosphate Dehydrogenase and Phosphoribulokinase. J Exp Bot. 2011;62(11):3799-805. PubMed PMID: 21498632.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - Inter-species variation in the oligomeric states of the higher plant Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase. AU - Howard,Thomas P, AU - Lloyd,Julie C, AU - Raines,Christine A, Y1 - 2011/04/15/ PY - 2011/4/19/entrez PY - 2011/4/19/pubmed PY - 2011/11/8/medline SP - 3799 EP - 805 JF - Journal of experimental botany JO - J. Exp. Bot. VL - 62 IS - 11 N2 - In darkened leaves the Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK) form a regulatory multi-enzyme complex with the small chloroplast protein CP12. GAPDH also forms a high molecular weight regulatory mono-enzyme complex. Given that there are different reports as to the number and subunit composition of these complexes and that enzyme regulatory mechanisms are known to vary between species, it was reasoned that protein-protein interactions may also vary between species. Here, this variation is investigated. This study shows that two different tetramers of GAPDH (an A2B2 heterotetramer and an A4 homotetramer) have the capacity to form part of the PRK/GAPDH/CP12 complex. The role of the PRK/GAPDH/CP12 complex is not simply to regulate the 'non-regulatory' A4 GAPDH tetramer. This study also demonstrates that the abundance and nature of PRK/GAPDH/CP12 interactions are not equal in all species and that whilst NAD enhances complex formation in some species, this is not sufficient for complex formation in others. Furthermore, it is shown that the GAPDH mono-enzyme complex is more abundant as a 2(A2B2) complex, rather than the larger 4(A2B2) complex. This smaller complex is sensitive to cellular metabolites indicating that it is an important regulatory isoform of GAPDH. This comparative study has highlighted considerable heterogeneity in PRK and GAPDH protein interactions between closely related species and the possible underlying physiological basis for this is discussed. SN - 1460-2431 UR - https://www.unboundmedicine.com/medline/citation/21498632/full_citation/Inter_species_variation_in_the_oligomeric_states_of_the_higher_plant_Calvin_cycle_enzymes_glyceraldehyde_3_phosphate_dehydrogenase_and_phosphoribulokinase_ L2 - https://academic.oup.com/jxb/article-lookup/doi/10.1093/jxb/err057 DB - PRIME DP - Unbound Medicine ER -