Enzyme kinetic study of the DEAD-box RNA helicase stimulated by the ubiquitin-like protein Hub1
หัวหน้าโครงการ
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สิทธินันท์ ชนะรัตน์
ทีมวิจัย
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สิทธินันท์ ชนะรัตน์
หัวหน้าโครงการ
ชิษณุสรร สวัสดิวัตน์
นักวิจัยที่ปรึกษา
วันที่เริ่มโครงการ
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2 พ.ค. 2561
วัตถุประสงค์
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Since fidelity of pre-mRNA splicing is monitored and controlled by RNA helicases, it is of importance to comprehend the underlying mechanism how the enzymes are regulated. Moreover, as Hub1 is the first identified co-factor of splicing-related DEAD-box helicases, understanding its regulatory role will shed light on enzyme manipulation and ultimately on splicing fidelity control as a therapeutic target for missplicing-related diseases. Specific objectives of this study include the following:
a) To clone, express and purify Prp5 helicase and Hub1 protein recombinantly in order to study enzymatic activity in vitro.
b) To test physical characteristics of the recombinantly purified Prp5 protein.
c) To determine Prp5 enzyme kinetics and the nucleotide binding affinity.
d) To ascertain how Hub1 influences physical properties, enzymatic activity, kinetics and nucleotide binding affinity of Prp5.
