Regulatory circuitry of RNA polymerase II c-terminal domain phosphatase Fcp1 in Saccharomyces cerevisiae

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In the cell, information essential for life is stored on the DNA in units called genes. Each gene contains the information required for the production of one protein, some of which are required at all times, while others only under certain conditions. As a result, control of protein production is a critical process for maintenance of normal cellular function. All protein production in the cell starts with a process called transcription during which a copy of the required gene is made. This is an important process because if the DNA template itself were to be used, the chances of damage and loss of vital information are greatly increased. RNA Polymerase II (RNAPII) is the enzyme responsible for the transcription of the majority of genes. It is different from other RNA polymerases as it contains a tail region called the C-terminal domain (CTD). The CTD functions like a port where proteins that work with RNAPII dock as required at different stages of transcription. The CTD must ensure that only the correct proteins bind at any given time as premature or delayed binding leads to unstable or non-functional DNA copies. The CTD achieves this is by changing its shape, allowing only correctly shaped proteins to fit at a given time. Fcp1 is a protein that aids in the CTD remodeling process at various stages of transcription. While the role of Fcp1 is known, how Fcp1 recognizes when to remodel the CTD remains unknown and will be the focus of this research proposal. We have performed a genetic screen focusing on genes already known to play a role in transcription regulation to identify possible Fcp1 regulators. We have generated a list of potential candidates to follow up on by looking at how inhibiting the function of these candidates leads to CTD remodeling defects and general transcription defects. We will also determine if their regulation of Fcp1 affects only specific genes or all genes. If only specific genes are affected, it will suggest that multiple proteins regulate Fcp1 function, requiring that we identify them to better understand how the transcription process is regulated by Fcp1.