We are interested in finding the amino acids and structural features which determine water permeability in the aquaporin (AQP) family of proteins and in the larger family of membrane intrinsic proteins (MIPs). We have expressed the AQP1 protein in yeast secretory vesicles and have also reconstituted yeast-expressed AQP1 into lipid vesicles. We have shown that the protein acts as a water channel in both environments. We are in the process of expressing AQP2 and AQP3 in the same yeast system. We have expressed two closely related proteins (FPS and GlpF) from the MIP family which, although homologous in sequence, do not act as water channels. We would like to find specific amino acids or protein domains which differ among the water channels and non-water channels and which may be important for determining water permeability. To do this, we plan to analyze the sequences and secondary structures of all of the MIP and AQP proteins and look for regions which are conserved or variable. Sites which potentially determine water permeability can then be evaluated experimentally using our yeast expression system. Sequence alignments and secondary structure predictions are possible with the CGC software package which is available from the Pittsburgh Supercomputing Center.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR006009-10
Application #
6221089
Study Section
Project Start
1999-08-01
Project End
2000-07-31
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
10
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Mellon Pitts Corporation (Mpc Corp)
Department
Type
DUNS #
City
Pittsburgh
State
PA
Country
United States
Zip Code
15213
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