人類的hHR23A和hHR23B基因與酵母菌Saccharomyces cerevisiae 的RAD23基因同源，這兩個因子都含有數個功能區域，包括N端的ubiquitin相似區域、兩個ubiquitin連結區域和XPC鍵結區域。先前的研究顯示hHR23B蛋白質與XPC蛋白質結合，在C型著色性亁皮症中有缺損的現象，並且參與核苷酸切除修復的過程，但是hHR23A的功能還不是很清楚。我們發現hHR23B蛋白的XPC鍵結區域能造成野生型hHR23B顯著抑制的外顯型，並且在寄主細胞再活化分析中部分抑制DNA修復系統的功能。相反地，hHR23A的XPC鍵結區域卻沒有類似的作用。這顯示了hHR23B參與全面性基因組修復（global genome repair）的路徑，而hHR23A則否。這個結果也利用穩定表達hHR23B XPC鍵結區域的NIH/3T3細胞株再作確認。在過去幾年中，干擾性RNA系統已建立為壓抑模式中很有效力的工具，無論是在活體內或體外的試驗。我們在hHR23A和hHR23B基因分別建構了三個干擾性RNA的建構物，試圖釐清hHR23A和hHR23B的功能。在HtTA1細胞中以西方墨點法分析，發現其中兩個hHR23A和其中一個hHR23B的建構物，能抑制內源性的hHR23A或hHR23B蛋白質的表現，並且也用RNA反轉錄聚合酶鏈鎖反應再作確認。此外，在hHR23A的ubiquitin連結區域中，將可能與ubiquitin結合的位置製造突變株，也將會測試它們被接上ubiquitin的能力。利用這些可能與ubiquitin相關的突變株，研究hHR23A在蛋白質降解和DNA修復中扮演的角色。

Human hHR23A and hHR23B genes are the homologues of Saccharomyces cerevisiae RAD23 gene and these two factors both contain functional domains including an ubiquitin-like (UBL) domain at the N-termini, two ubiquitin-associated (UBA) domains and an XPC-binding domain. Previous studies showed that the hHR23B protein is complexed with the XP group C (XPC) protein, defective in the xeroderma pigmentosum C syndrome, and is involved in the global genome nucleotide excision repair (NER) pathway, but the functions of hHR23A remain to be elucidated. We found that the XPC-binding domain of hHR23B contributes to a dominant negative phenotype for the wild-type hHR23B protein and partially inhibits the function of repair system by the host cell reactivation (HCR) assay. On the contrary, the XPC-binding domain of hHR23A didn’t exhibit such an effect. It indicated that only hHR23B participates in global genome repair (GGR) pathway, but hHR23A does not. These data have been confirmed in NIH/3T3 cells stably transfected with the XPC-binding domain of the hHR23B. In past years, RNA interference (RNAi) system has been a powerful tool to establish knock-down models in vitro and in vivo. We constructed three RNAi constructs of each of the hHR23A or hHR23B genes, attempting to clarify the functions of hHR23A/hHR23B. In our data, two of the hHR23A and one hHR23B constructs inhibited endogenous levels of the hHR23A or hHR23B in HtTA1 cells, assayed by Western blot. These data have been confirmed by RT-PCR. In addition, the UBA domains of hHR23A/hHR23B are presumably ubiquitinated. The mutants in potential ubiquitination sites on UBA domains of hHR23A will therefore be examined for their ubiquitination activities. Using these potential ubiquitination mutants, the hHR23A would be studied for their roles in proteolysis and DNA repair.

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