The Fungal Hydrophobin RolA Bound on Hydrophobic Surfaces Recruits Esterase.

Toru Takahashi1, Hiroshi Maeda 2, Sachiyo Yoneda 1, Shinsaku Ohtaki1, Yohei Yamagata 1,2, Fumihiko Hasegawa 2, Katsuya Gomi 1,2, Tasuku Nakajima 1,2, and Keietsu Abe 1,2,*,

Author address: 

1Grad. Sch, of Agricul. Science, 2The New Indust. Creat.Hatchery Cent., Tohoku Univ., Sendai, Japan

Abstract: 

W hen fungi grow on plant or insect surfaces coated with wax polyesters as protectants against pathogens, the fungi generally form aerial hyphae to contact the surfaces. Hydrophobins, which are surface-active proteins found in fungi, coat aerial structures such as hyphae or conidiophores and are involved in adhesion to hydrophobic surfaces. W hen an industrial fungus Aspergillus oryzae was cultivated in liquid medium containing the biodegradable polyester polybutylene succinate-coadipate (PBSA), the hydrophobin RolA and cutinase CutL1, which hydrolyzes PBSA, were simultaneously expressed. High levels of RolA and its localization on the cell surface in the presence of PBSA were confirmed by immunostaining. Preincubation of PBSA with RolA stimulated PBSA degradation by CutL1, suggesting that RolA bound to a PBSA surface was required for the stimulation. Immunostaining revealed that PBSA films coated with RolA specifically adsorbed CutL1. Quartz crystal microbalance analyses further demonstrated that RolA attached to a hydrophobic sensor chip specifically adsorbed CutL1. These results suggest that RolA adsorbed to the hydrophobic surface of PBSA recruits CutL1, resulting in condensation of CutL1 on the PBSA surface and consequent stimulation of PBSA hydrolysis.
2005

abstract No: 

214.

Full conference title: 

23rd Fungal Genetics Conference
    • Fungal Genetics Conference 23rd (2002)