銀葉病菌由来プロエンドポリガラクツロナーゼIのC末端44残基による自己不活性化

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  • Auto-inactivation of Stereum purpureum Proendopolygalacturonase I by C-terminal 44 Amino Acid Residues
  • Auto-inactivation of Stereum purpureum proendopolygalacturonase 1 by C-terminal 44 amino acid residues

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The pro-form (Pro-EndoPG I) of Stereum purpureum endopolygalacturonase I has a unique C-terminal region (pro-sequence) that is lacking in PGs of other origins. Mature EndoPG I purified from the culture filtrate of this fungus does not have the 44-amino-acid pro-sequence present in Pro-EndoPG I. We expressed Pro-EndoPG I in Escherichia coli and examined its activity. It was found that Pro-EndoPG I had no PG activity initially but some was acquired after the degradation of a portion of the pro-sequence with V8 protease. These results suggest that the pro-sequence inactivates auto-PG activity. No similar characteristic has been reported for any glycoside hydrolase. We then constructed C-terminal deletion mutants of Pro-EndoPG I and showed that 31 or 32 residues of the 44 amino acid residues in the pro-sequence were needed for the inactivation. Furthermore, we identified two Glu residues, E364 and E366, that were also related to the auto-inactivation. A test involving injection of the enzyme into apple trees showed that Pro-EndoPG I induced the same silver-leaf symptoms as mature EndoPG I. It is assumed that the Pro-EndoPG I was activated with plant proteases.

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