Journal
FUNGAL GENETICS AND BIOLOGY
Volume 42, Issue 11, Pages 924-934Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.fgb.2005.08.002
Keywords
aspartic protease; biocontrol; expressed sequence tags; filamentous fungi proteomics; gene expression; LC/MS-MS; MALDI-TOF; mycoparasitism; Trichoderma harzianum
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Trichoderma mycoparasitic activity depends on the secretion of complex mixtures of hydrolytic enzymes able to degrade the host cell wall. We have analysed the extracellular proteome secreted by T harzianum CECT 2413 in the presence of different fungal cell walls. Significant differences were detected in 2DE maps, depending on the use of specific cell walls or chitin. A combination of MALDI-TOF and liquid chromatography mass spectrometry allowed the identification of a novel aspartic protease (P6281: MW 33 and pl 4.3) highly induced by fungal cell walls. A broad EST library from T harzianum CECT 2413 was used to obtain the full-length sequence. The protein showed 44% identity with the polyporopepsin (EC 3.4.23.29) from the basidiomycete Irpex lacteus. Lower identity percentages were found with other pepsin-like proteases from filamentous fungi (< 31%) and animals (< 29%). Northern blot and promoter sequence analyses support the implication of the protease P6281 in mycoparasitism. (c) 2005 Elsevier Inc. All rights reserved.
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