Literature DB >> 17015001

Two families of extracellular phospholipase C genes are present in aspergilli.

Danny Tuckwell1, Sandra E Lavens, Mike Birch.   

Abstract

Fungi secrete extracellular enzymes to enable them to harvest nutrients from the environment. In the case of pathogenic fungi these enzymes can also be pathogenesis factors. Here we report the identification in fungi of a complex family of extracellular phospholipase C (PLC) enzymes, homologous to the Pseudomonas aeruginosa PLCH_PSEAE. Database searches and phylogenetic analysis showed that the PLCs clustered into two groups with different evolutionary histories. One group, subdivided into PLC-A, -B, -C and -D, was found only in aspergilli and Neosartorya fischeri. Each species only ever showed three of the four PLCs except N. fischeri which had all four PLCs plus duplicate PLC-A, -B and -C genes. Modelling studies indicated that these PLCs had mechanistic similarities to phosphoesterases and aryl sulphatases, but that they probably did not differ in substrate specificity. The second group, PLC-E, was seen in a wider range of fungi including some species of aspergilli and was always found in a head-to-head arrangement with a copper oxidase, similar to the laccases. The PLC genes appear to have arisen from separate gene transfer events from bacteria or lower eukaryotes. Thus, aspergilli have acquired PLCs twice in the course of evolution.

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Year:  2006        PMID: 17015001     DOI: 10.1016/j.mycres.2006.07.013

Source DB:  PubMed          Journal:  Mycol Res        ISSN: 0953-7562


  1 in total

1.  Role of phospholipase C and protein kinase C in Aspergillus nidulans during growth on pectin or glucose: Effects on germination and duplication cycle.

Authors:  M A S C Chellegatti; P D Yuvamoto; S Said
Journal:  Folia Microbiol (Praha)       Date:  2010-06-06       Impact factor: 2.099

  1 in total

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