| Summary: | 碩士 === 國立陽明大學 === 遺傳學研究所 === 89 === According to the previous finding of our laboratory, the ribosomal protein L7 is responsible for binding to the ER membrane. In this thesis, I examine the binding region of ribosomal protein L7 and determine the binding affinity to the ER. The results show that the NH2 terminal region of ribosomal protein L7 makes up a tandem repeated sequence and is essential for binding to the ER membrane. Using a biosensor assay, the dissociation equilibrium constant (KD) of the NH2 terminal tandem repeated sequence to bind to the ER is 2.89 x 10-8 M which is similar to the binding affinity of ribosome, suggesting that this sequence involves in the formation of rough ER. In the same assay, no significant difference in binding affinity to the ER is found for modified proteins regardless the number of repeated units, but protein without any repeated unit does not bind, suggesting that the repeated unit alone rather the number of copies is important to bind. This study suggests that the tandem repeated sequence of the ribosomal protein L7 does not itself intrinsically interact with the ribosomal components but externally engages in binding with the ER membrane assisting the ribosome in the formation of rough ER.
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