MutM Interaction Partners Detected in Mycobacterium smegmatis by Tandem Affinity Purification

分类： 生物学 >> 生物物理学 >> 生物物理、生物化学与分子生物学 提交时间： 2016-05-12

Fan Shang-Hua Yu Zi-Niu Fan Shang-Hua Zhou Ying Zhang Hong-Tai Fleming, Joy Zhang Xian-En Bi Li-Jun Fan Shang-Hua Zhou Ying Zhang Hong-Tai Fleming, Joy Zhang Xian-En Bi Li-Jun

摘要： MutM (Formamidopyrimidine-DNA glycosylase, Fpg), a bifunctional base excision repair enzyme (DNA glycosylase/AP lyase), is involved in the repair of many kinds of DNA damage, including the formation of 8-oxoguanine, 5-formyluracil, and C/C mismatches, through recognizing DNA damage and removing damaged bases. The mechanisms of MutM involvement, however, with the exception of 8-oxoG, are poorly understood. Here, we identified proteins which interact with MutM in Mycobacterium smegmatis using methods of tandem affinity purification and mass spectrometry and used Far-western and GST pull-down analysis to validate the interactions between MutM and DEAD-box rna helicase, RpsC, and UvrA. Results demonstrated that tandem affinity purification is a suitable method for identifying MutM interacting proteins and provided insights into the mechanism by which MutM is involved in DNA damage repair.

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