Identification and characterization of a tri-partite hydrophobin from Claviceps fusiformis . A novel type of class II hydrophobin

@article{citeulike:2698922, abstract = {A new type of hydrophobin is encoded by an abundant mRNA of Claviceps fusiformis. The predicted amino-acid sequence of the protein, dubbed CFTH1, shows a putative signal sequence for secretion, followed by three class II hydrophobin domains each preceded by glycine/asparagine rich regions. SDS/PAGE analysis of 60\% ethanol extractions of C. fusiformis mycelia from shaken cultures showed CFTH1 at the 50-55-kDa position. N-terminal sequencing of both untreated mature CFTH1 and of a fragment obtained by trypsin digestion revealed that CFTH1 is not processed between the hydrophobin domains. Mass spectroscopy showed a mass of about 36 500 Da, which is about 1500 Da higher than the mass predicted from the constituent amino acids, indicating post-translational modification but not glycosylation. Purified CFTH1 self-assembled at hydrophilic/hydrophobic interfaces and, after assembly at a water/air interface, it was found to be highly surface active. Antibodies raised against CFTH1 localized the protein in a mucilageous coat surrounding submerged vegetative hyphae in liquid shaken culture and, as a discrete layer of about 10 nm thickness at the surface of aerial hyphae of standing cultures, suggesting a role in the formation of aerial hyphae.}, author = {de Vries, Onno M. H. and Moore, Sabine and Arntz, Claudia and Wessels, Joseph G. H. and Tudzynski, Paul }, citeulike-article-id = {2698922}, doi = {http://dx.doi.org/10.1046/j.1432-1327.1999.00387.x}, journal = {European Journal of Biochemistry}, number = {2}, pages = {377--385}, posted-at = {2008-05-21 14:52:13}, priority = {2}, title = {Identification and characterization of a tri-partite hydrophobin from Claviceps fusiformis . A novel type of class II hydrophobin}, url = {http://dx.doi.org/10.1046/j.1432-1327.1999.00387.x}, volume = {262}, year = {1999} }

TY - JOUR ID - citeulike:2698922 L3 - citeulike-article-id:2698922 TI - Identification and characterization of a tri-partite hydrophobin from Claviceps fusiformis . A novel type of class II hydrophobin JF - European Journal of Biochemistry VL - 262 IS - 2 SP - 377 EP - 385 N2 - A new type of hydrophobin is encoded by an abundant mRNA of Claviceps fusiformis. The predicted amino-acid sequence of the protein, dubbed CFTH1, shows a putative signal sequence for secretion, followed by three class II hydrophobin domains each preceded by glycine/asparagine rich regions. SDS/PAGE analysis of 60% ethanol extractions of C. fusiformis mycelia from shaken cultures showed CFTH1 at the 50-55-kDa position. N-terminal sequencing of both untreated mature CFTH1 and of a fragment obtained by trypsin digestion revealed that CFTH1 is not processed between the hydrophobin domains. Mass spectroscopy showed a mass of about 36 500 Da, which is about 1500 Da higher than the mass predicted from the constituent amino acids, indicating post-translational modification but not glycosylation. Purified CFTH1 self-assembled at hydrophilic/hydrophobic interfaces and, after assembly at a water/air interface, it was found to be highly surface active. Antibodies raised against CFTH1 localized the protein in a mucilageous coat surrounding submerged vegetative hyphae in liquid shaken culture and, as a discrete layer of about 10 nm thickness at the surface of aerial hyphae of standing cultures, suggesting a role in the formation of aerial hyphae. AU - de Vries, Onno AU - Moore, Sabine AU - Arntz, Claudia AU - Wessels, Joseph AU - Tudzynski, Paul PY - 1999/// UR - http://dx.doi.org/10.1046/j.1432-1327.1999.00387.x ER -