MutM interaction partners detected in Mycobacterium smegmatis by tandem affinity purification

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

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)935-946
Number of pages12
JournalProgress in Biochemistry and Biophysics
Issue number10
StatePublished - Oct 2015
Externally publishedYes


  • BER
  • MutM
  • Mycobacterium smegmatis
  • TAP

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry


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