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Enzyme-enzyme interaction in the chloroplast: Glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase

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Abstract

Apparent physical interaction between pea chloroplast (Pisum sativum L.) glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13) and aldolase (EC 4.1.2.13) is seen in phase-partitioning, fluorescent-anisotropy and isoelectric-focusing experiments. Similarly, results obtained in phase-partitioning and isoelectric-focusing experiments indicate physical interaction between aldolase and triose-phosphate isomerase (EC 5.3.1.1). Kinetic experiments suggest that both aldolase-bound glyceraldehyde-3-phosphate and triose-phosphate isomerase bound glyceraldehyde-3-phosphate can act as substrate for glyceraldehyde-3-phosphate dehydrogenase. These results are consistent with the notion that there is interaction between these three enzymes both during photosynthetic CO2 fixation and during glycolysis in the chloroplast.

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Abbreviations

FITC:

fluorescein isothiocyanate

glyceraldehyde3-P:

glyceraldehyde-3-phosphate

K:

partition coefficient

K m (ALD):

apparent K m value obtained when aldolase levels are varied

K m (GAP):

K m value obtained when glyceraldehyde-3-P concentrations are varied

K m (PGK):

apparent K m value obtained when phosphoglycerate kinase levels are varied

K m (TPI):

apparent K m value obtained when triose-P isomerase levels are varied

PEG:

polyethyleneglycol

Rubisco:

ribulose-1,5-bisphosphate carboxylase/oxygenase

triose-P:

triose phosphate

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Authors and Affiliations

  1. Department of Biological Sciences, University of Illinois at Chicago, 845 West Taylor St., 60607-7060, Chicago, IL, USA

    Louise E. Anderson, Ilana M. Goldhaber-Gordon, Dong Li, Minghui Xiang & Namita Prakash

  2. Shanghai Institute of Plant Physiology, Academia Sinica, 200032, Shanghai, China

    Xiao-yi Tang

Authors
  1. Louise E. Anderson
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  2. Ilana M. Goldhaber-Gordon
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  3. Dong Li
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  4. Xiao-yi Tang
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  5. Minghui Xiang
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  6. Namita Prakash
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Corresponding author

Correspondence to Louise E. Anderson.

Additional information

We thank Fred J. Stevens, Argonne National Laboratory, for help in analysis of the tertiary structures, Göte Johansson, University of Lund, for hosting two of us in his laboratory where we did the initial phase-partitioning experiments, Chang-hou Li, Shanghai Research Centre of Biotechnology, for the use of the fluorimeter, Lawrence Sykora and the University of Illinois greenhouse staff for growing the pea plants, Jack T. Gibbons for electron microscopy, and Christie Aljets, Xua Ming Da, Xiang He, Arif Ali Khan, Fang Luo, Martha Pacold, Michael Pacold, Lei Shi, Hyun Moon Shin and Qi Zhao for their assistance with these experiments. Support came from the University of Illinois-Chicago Research Board, the US National Science Foundation (Grants DCB 9018265, INT 91-15490 and INT 91-13311) and the Chinese National Science Foundation (Grant 39230050).

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Anderson, L.E., Goldhaber-Gordon, I.M., Li, D. et al. Enzyme-enzyme interaction in the chloroplast: Glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase. Planta 196, 245–255 (1995). https://doi.org/10.1007/BF00201381

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  • DOI: https://doi.org/10.1007/BF00201381

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