Hydrophobins: Multipurpose proteins

Authors
Citation
Hab. Wosten, Hydrophobins: Multipurpose proteins, ANN R MICRO, 55, 2001, pp. 625-646
Citations number
102
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Microbiology
Journal title
ANNUAL REVIEW OF MICROBIOLOGY
ISSN journal
0066-4227 → ACNP
Volume
55
Year of publication
2001
Pages
625 - 646
Database
ISI
SICI code
0066-4227(2001)55:<625:HMP>2.0.ZU;2-O
Abstract
Class I and class II hydrophobins are small secreted fungal proteins that p lay a role in a broad range of processes in the growth and development of f ilamentous fungi. For instance, they are involved in the formation of aeria l structures and in the attachment of hyphae to hydrophobic surfaces. The m echanisms by which hydrophobins fulfill these functions are based on their property to self-assemble at hydrophilic-hydrophobic interfaces into a 10 n m-thin highly amphipathic film. Complementation studies have shown that cla ss I hydrophobins belong to a closely related group of morphogenetic protei ns, but that they have evolved to function at specific interfaces. Recent e vidence indicates that hydrophobins do not only function by self-assembly. Monomeric hydrophobin has been implicated in cell-wall assembly, but the un derlying mechanism is not yet clear. In addition, hydrophobin monomers coul d act as toxins and elicitors.