Abstract
In yeasts proliferation of microbodies (glyoxysomes/peroxisomes) is largely prescribed by the growth environment and due to the fact that the organelles harbour essential enzymic functions required for the metabolism of the carbon and/or nitrogen source. Presently activities of more than 20 different enzymes have been shown to reside in yeast microbodies namely catalase, several H202-producing oxidases and enzymes involved in 8-oxidation, glyoxylate cycle enzymes, dehydrogenases, an amino transferase and a transketolase. The functioning of these organelles often requires extensive metabolic interactions with other cell compartments such as mitochondria, microsomes or the cyrosol.
All available evidence indicates that yeast microbodies do not arise from the ER or de novo but develop from already existing organelles. Synthesis of microbody-matrix enzymes appears to be mainly controlled at the transcriptional level and takes place on cytosolic polysomes. Microbody-protein subunits (both matrix and membrane proteins) are synthesized in their mature form and are imported post-translationally. Topogenic signals for directing yeast microbody proteins to their target organelle are contained within their structure and are probably universal.
Yeast microbodies have been shown to be acidic in nature with an internal pH of 5.8 – 6.0 whereas the cytosolic pH is approximately 7.1. This electrochemical proton gradient — generated by a membrane bound H+-ATPase — may play an important role in different transport processes across the peroxisomal membrane including uptake of matrix proteins and transport of low molecular weight compounds such as substrates and/or metabolic intermediates.
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Veenhuis, M., Harder, W. (1987). Metabolic Significance and Biogenesis of Microbodies in Yeasts. In: Fahimi, H.D., Sies, H. (eds) Peroxisomes in Biology and Medicine. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71325-5_47
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DOI: https://doi.org/10.1007/978-3-642-71325-5_47
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