The ability to explore, detect and modify the protein features of cell surfaces is a key in the long-term development of many diagnostic and therapeutic strategies. A major obstacle is the fact that the fundamental nature of protein-membrane interactions is largely unknown. Two model systems have been developed for using molecular genetics to determine the principles regulating such interactions: the lysis control genes S of bacteriophage lambda and E of bacteriophage PhiX174. These genes are small (S = 107 codons, E = 91 codons) and lethal, and thus are well-suited for mutational analysis. In vitro mRNA and protein synthesis will be sued to characterize both individually and in pairs representatives from a collection of about 50 missense S mutants in terms of membrane interaction and protease accessibility. Intragenic suppressors of many of these S mutants will be isolated and sequenced to determine interaction domains within the polypeptide. The novel translational control system of S will be probed by site-directed mutagenesis, to determine the parameters by which the two different protein products are synthesized in regulated proportion. The E gene will be subjected to fine structure lac fusion analysis and reversion studies to determine the minimum requirements for membrane insertion of the polypeptide. A missense analysis of the E gene will be carried out in the same way done successfully for the S cistron.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM027099-10
Application #
3274519
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1980-01-01
Project End
1991-12-31
Budget Start
1989-01-01
Budget End
1989-12-31
Support Year
10
Fiscal Year
1989
Total Cost
Indirect Cost
Name
Texas A&M University
Department
Type
Schools of Medicine
DUNS #
City
College Station
State
TX
Country
United States
Zip Code
77845
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