Gene cloning, molecular modeling, and phylogenetics of serine protease P32 and serine carboxypeptidase SCP1 from nematophagous fungi Pochonia rubescens and Pochonia chlamydosporia

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Title: Gene cloning, molecular modeling, and phylogenetics of serine protease P32 and serine carboxypeptidase SCP1 from nematophagous fungi Pochonia rubescens and Pochonia chlamydosporia
Authors: Larriba Tornel, Eduardo | Martín-Nieto, José | Lopez-Llorca, Luis Vicente
Research Group/s: Genética Humana y de Mamíferos (GHM)
Center, Department or Service: Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología
Keywords: Nematophagous fungi | Pochonia spp. | Serine protease | Serine carboxypeptidase | Phylogenesis
Knowledge Area: Genética | Microbiología
Issue Date: 12-Jun-2012
Publisher: NRC Research Press
Citation: LARRIBA, Eduardo; MARTÍN-NIETO, José; LOPEZ-LLORCA, Luis Vicente. “Gene cloning, molecular modeling, and phylogenetics of serine protease P32 and serine carboxypeptidase SCP1 from nematophagous fungi Pochonia rubescens and Pochonia chlamydosporia”. Canadian Journal of Microbiology. Vol. 58, No. 7 (July 2012). ISSN 0008-4166, pp. 815-827
Abstract: The fungi Pochonia chlamydosporia and Pochonia rubescens are parasites of nematode eggs and thus are biocontrol agents of nematodes. Proteolytic enzymes such as the S8 proteases VCP1 and P32, secreted during the pathogenesis of nematode eggs, are major virulence factors in these fungi. Recently, expression of these enzymes and of SCP1, a new putative S10 carboxypeptidase, was detected during endophytic colonization of barley roots by these fungi. In our study, we cloned the genomic and mRNA sequences encoding P32 from P. rubescens and SCP1 from P. chlamydosporia. P32 showed a high homology with the serine proteases Pr1A from the entomopathogenic fungus Metarhizium anisopliae and VCP1 from P. chlamydosporia (86% and 76% identity, respectively). However, the catalytic pocket of P32 showed differences in the amino acids of the substrate-recognition sites compared with the catalytic pockets of Pr1A and VCP1 proteases. Phylogenetic analysis of P32 suggests a common ancestor with protease Pr1A. SCP1 displays the characteristic features of a member of the S10 family of serine proteases. Phylogenetic comparisons show that SCP1 and other carboxypeptidases from filamentous fungi have an origin different from that of yeast vacuolar serine carboxypeptidases. Understanding protease genes from nematophagous fungi is crucial for enhancing the biocontrol potential of these organisms.
Sponsor: This research was funded by the Spanish Ministry of Science and Innovation grants AGL2008-00716/AGR and AGL2011-29297.
URI: http://hdl.handle.net/10045/26551
ISSN: 0008-4166 (Print) | 1480-3275 (Online)
DOI: 10.1139/W2012-054
Language: eng
Type: info:eu-repo/semantics/article
Rights: © 2012 NRC Research Press
Peer Review: si
Publisher version: http://dx.doi.org/10.1139/W2012-054
Appears in Collections:INV - GHM - Artículos de Revistas
INV - Fitopatología - Artículos de Revistas

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