Aquaporin and aquaglyceroporins in Aspergillus nidulans are dispensable in osmotic stress responses.

Dong-Soon Oh, Hanyan Lu, Kap-Hoon Han

Author address: 

Woosuk University

Abstract: 

Aquaporin is a water channel protein found in almost all organisms from bacteria to human. More than 200 members of this family were identified up to date. There are two major categories of Major Intrinsic Protein (MIP) channels, aquaporins and glycerol facilitators, which facilitate the diffusion across biological membranes of water or glycerol and other uncharged compounds, respectively. The full genome sequencing of various fungal species revealed that there are 3 to 5 aquaporins in their genome. However, no functional characteristics were studied so far in Aspergillus sp. In Aspergillus nidulans, one orthodox aquaporin (aqpA) and four aquaglyceroporins (aqpB~E) were found in the genome. Knock8208;out of each aquaporin or aquaplyceroporin didn’t show obvious phenotypic change in osmotic stress, suggesting that the function of the genes may be redundant or not be related in osmotic stress responses. However, resistance of fluconazol has been changed in some mutants, indicating that the function of aquaporins play roles in susceptibility of antifungal reagent. [This work was supported by NRF Korea (20098208;0072920)]
2012

abstract No: 

PR7.21

Full conference title: 

11 th European Conference on Fungal Genetics
    • ECFG 11th (2012)