Related Experiment Videos
Structure-function relationships of the chicken progesterone receptor.
O M Conneely1, A D Dobson, M A Carson
1Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030.
Biochemical Society Transactions
|October 1, 1988
Summary
Chicken progesterone receptor (CPR) A and B proteins originate from a single mRNA. Functional domains include DNA binding and gene activation in the central region, and hormone binding in the C-terminal region.
Area of Science:
- Molecular Biology
- Endocrinology
- Genetics
Background:
- The chicken progesterone receptor (CPR) plays a crucial role in gene regulation.
- Understanding the functional domains and protein origins of CPR is essential for deciphering its mechanism of action.
Purpose of the Study:
- To define the functional domains of the chicken progesterone receptor (CPR).
- To establish the origin of the CPR A and B proteins.
Main Methods:
- Cloning and sequencing of the complete cDNA encoding CPR.
- Construction and analysis of deletion mutants in the receptor A cDNA.
Main Results:
- CPR A and B proteins are generated from a single mRNA transcript via alternate translation initiation.
- DNA binding and gene activator regions are located in the central portion of the CPR protein.
- The hormone binding domain is situated in the C-terminal region of CPR.
- Hormone binding domain interaction modulates the target gene activator site.
Conclusions:
- The CPR protein exhibits distinct functional domains crucial for its activity.
- Alternate translation initiation from a single mRNA is the mechanism for CPR A and B protein production.
- The structure-function relationship of CPR is elucidated, highlighting domain interactions.