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Production of Organic Acids

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Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

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Physarum polymalic acid hydrolase: Recombinant expression and enzyme activation.

Wolfgang Mueller¹, Markus Haindl, Eggehard Holler

¹Biophysik und Physikalische Biochemie, Universitaet Regensburg, 93040 Regensburg, Germany.

Biochemical and Biophysical Research Communications

|October 11, 2008

Summary

Polymalic acid and its hydrolase from slime mold are key for nanoconjugate drug delivery. Protein tyrosine phosphorylation activates the hydrolase and inhibits synthesis, suggesting a response to membrane damage.

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Area of Science:

Biochemistry
Cell Biology
Biotechnology

Background:

Polymalic acid (PMA) from Physarum polycephalum is a platform for nanoconjugate synthesis in antitumor drug delivery.
PMA is secreted via a specific exohydrolase, PMA hydrolase, which is expressed in an inactive form.
The inactive hydrolase acts as a molecular adapter for PMA trafficking within the plasmodium.

Purpose of the Study:

To investigate the activation mechanism of Physarum polycephalum PMA hydrolase.
To explore the role of protein tyrosine phosphorylation in PMA hydrolase activation and PMA synthesis.
To understand the signaling response to plasma membrane damage in P. polycephalum.

Main Methods:

Purification of PMA and its exohydrolase from Physarum polycephalum plasmodium cultures.
Recombinant expression of inactive Physarum PMA hydrolase in yeast Saccharomyces.
Activation of purified inactive hydrolase using plasma membrane fragments from P. polycephalum.

Main Results:

Physarum PMA hydrolase is activated during secretion following specific protein tyrosine phosphorylation and dissociation from plasma membranes.
Recombinantly expressed inactive hydrolase can be activated on a preparative basis by P. polycephalum plasma membrane fragments.
Activation of PMA hydrolase and inhibition of PMA synthesis are complementary events mediated by protein tyrosine phosphorylation.

Conclusions:

Protein tyrosine phosphorylation is a key regulatory mechanism for PMA hydrolase activation and PMA synthesis in Physarum polycephalum.
These phosphorylation events suggest a coordinated cellular response to plasma membrane damage.
The findings provide insights into the biotechnological application of PMA and its hydrolase in nanoconjugate drug delivery systems.