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Volume 150, Issue 7

An aspartic proteinase gene family in the filamentous fungus contains members with novel features Free

Abstract

, an important fungal plant pathogen, secretes aspartic proteinase (AP) activity in axenic cultures. No cysteine, serine or metalloproteinase activity could be detected. Proteinase activity was higher in culture medium containing BSA or wheat germ extract, as compared to minimal medium. A proportion of the enzyme activity remained in the extracellular glucan sheath. AP was also the only type of proteinase activity in fluid obtained from -infected tissue of apple, pepper, tomato and zucchini. Five genes encoding an AP were cloned and denoted . Features of the encoded proteins are discussed. BcAP1, especially, has novel characteristics. A phylogenetic analysis was performed comprising sequences originating from different kingdoms. BcAP1 and BcAP5 did not cluster in a bootstrap-supported clade. BcAP2 clusters with vacuolar APs. BcAP3 and BcAP4 cluster with secreted APs in a clade that also contains glycosylphosphatidylinositol-anchored proteinases from and . All five genes are expressed in liquid cultures. Transcript levels of , , and are subject to glucose and peptone repression. Transcripts from all five genes were detected in infected plant tissue, indicating that at least part of the AP activity originates from the pathogen.

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): AP, aspartic proteinase , CF, cell-free culture filtrate and Hb, haemoglobin
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2004-07-01
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An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features
Microbiology 150, 2475 (2004); https://doi.org/10.1099/mic.0.27058-0
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