Transcriptional analysis of the lichenase-like gene cel12A of the filamentous fungus Stachybotrys atra BP-A and its relevance for lignocellulose depolymerization.


Journal

International microbiology : the official journal of the Spanish Society for Microbiology
ISSN: 1618-1905
Titre abrégé: Int Microbiol
Pays: Switzerland
ID NLM: 9816585

Informations de publication

Date de publication:
May 2021
Historique:
received: 31 07 2020
accepted: 14 12 2020
revised: 03 11 2020
pubmed: 7 1 2021
medline: 27 8 2021
entrez: 6 1 2021
Statut: ppublish

Résumé

To rationally optimize the production of industrial enzymes by molecular means requires previous knowledge of the regulatory circuits controlling the expression of the corresponding genes. The genus Stachybotrys is an outstanding producer of cellulose-degrading enzymes. Previous studies isolated and characterized the lichenase-like/non-typical cellulase Cel12A of S. atra (AKA S. chartarum) belonging to glycosyl hydrolase family 12 (GH12). In this study, we used RT-qPCR to determine the pattern of expression of cel12A under different carbon sources and initial ambient pH. Among the carbon sources examined, rice straw triggered a greater increase in the expression of cel12A than 1% lactose or 0.1% glucose, indicating specific induction by rice straw. In contrast, cel12A was repressed in the presence of glucose even when combined with this inducer. The proximity of 2 adjacent 5'-CTGGGGTCTGGGG-3' CreA consensus target sites to the translational start site of cel12A strongly suggests that the carbon catabolite repression observed is directly mediated by CreA. Ambient pH did not have a significant effect on cel12A expression. These findings present new knowledge on transcriptional regulatory networks in Stachybotrys associated with cellulose/hemicellulose depolymerization. Rational engineering of CreA to remove CCR could constitute a novel strategy for improving the production of Cel12A.

Identifiants

pubmed: 33404932
doi: 10.1007/s10123-020-00155-9
pii: 10.1007/s10123-020-00155-9
doi:

Substances chimiques

Fungal Proteins 0
lignocellulose 11132-73-3
Cellulose 9004-34-6
Lignin 9005-53-2
Glycoside Hydrolases EC 3.2.1.-
licheninase EC 3.2.1.73
Glucose IY9XDZ35W2

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

197-205

Subventions

Organisme : Generalitat Valenciana
ID : PROMETEO/2018/066

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Auteurs

Pere Picart (P)

Department of Microbiology, Faculty of Biology, University of Barcelona, Avinguda Diagonal 643, 08028, Barcelona, Spain.

F I Javier Pastor (FIJ)

Department of Microbiology, Faculty of Biology, University of Barcelona, Avinguda Diagonal 643, 08028, Barcelona, Spain. fpastor@ub.es.

Margarita Orejas (M)

Instituto de Agroquímica y Tecnología de Alimentos, Consejo Superior de Investigaciones Científicas (IATA-CSIC), Avda. Agustín Escardino 7, 46980, Paterna, Valencia, Spain. morejas@iata.csic.es.

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Classifications MeSH