PcExl1 a novel acid expansin-like protein from the plant pathogen Pectobacterium carotovorum, binds cell walls differently to BsEXLX1

• Published in: PloS one 2014-04, Vol.9 (4), p.e95638-e95638
• Main Authors: Olarte-Lozano, Miguel, Mendoza-Nuñez, Mario A, Pastor, Nina, Segovia, Lorenzo, Folch-Mallol, Jorge, Martínez-Anaya, Claudia
• Format: Article
• Language: English
• Subjects: Bacillus subtilis; Bacteria, Phytopathogenic; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Binding; Biology and Life Sciences; Botanical research; Cell Wall - metabolism; Cell walls; Cellulase; Cellulose; Cellulose - metabolism; Cloning, Molecular; Enzymes; Filter paper; Gene Expression; Glycoside Hydrolases; Hydrolysis; Infections; Loosening; Medicine and Health Sciences; Microbiological research; Microorganisms; Models, Molecular; Mutagenesis; Pathogens; Pectobacterium carotovorum; Pectobacterium carotovorum - genetics; Pectobacterium carotovorum - metabolism; Physiology; Plant Cells - metabolism; Plant Cells - microbiology; Protein Binding; Protein Conformation; Proteins; Recombinant Proteins; Species Specificity; Static Electricity; Substrate Specificity; Wheat
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0095638

Microbial expansins act on plant cell walls similarly to plant expansins, albeit their loosening activity levels are tenfold lesser compared to plant expansins. We report the characterization of an expansin-like gene from the plant pathogen Pectobacterium carotovorum, named exl1. PcExl1 is an acidic protein that binds cellulose (Avicel), and weakens filter paper. The acidic nature of PcExl1 confers different binding properties when compared to Bacillus subtilis BsEXLX1, which is a basic protein. PcExl1 binding to wheat cell wall increased when acidic components were depleted, reaching a similar level to the binding to Avicel, indicating that cellulose is the target of PcExl1.