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Mgm101 Is a Rad52-related Protein Required for Mitochondrial DNA Recombination*
- MacMillan Mbantenkhu, Xiaowen Wang, Xin Jie Chen
- BiologyThe Journal of Biological Chemistry
- 25 October 2011
It is shown that the yeast mitochondrial nucleoid protein, Mgm101, is related to the Rad52-type recombination proteins that are widespread in organisms from bacteriophage to humans.
A Properly Configured Ring Structure Is Critical for the Function of the Mitochondrial DNA Recombination Protein, Mgm101*
- J. Nardozzi, Xiaowen Wang, MacMillan Mbantenkhu, S. Wilkens, Xin Jie Chen
- BiologyThe Journal of Biological Chemistry
- 4 September 2012
The structural elements that contribute to this distinctive higher order structural organization of Mgm101, including a pair of vicinal cysteines, were investigated and its functional implications were examined, finding that a properly configured ring structure is essential for Mgm 101 function in vivo.
Preparation of the Mgm101 recombination protein by MBP-based tagging strategy.
- Xiaowen Wang, MacMillan Mbantenkhu, S. Wierzbicki, Xin Jie Chen
- BiologyJournal of visualized experiments : JoVE
- 25 June 2013
A reliable procedure for the preparation of recombinant Mgm101 is described and may be used for the Preparation of other large oligomeric DNA-binding proteins that may be misfolded and toxic to bacterial cells.
A short carboxyl-terminal tail is required for single-stranded DNA binding, higher-order structural organization, and stability of the mitochondrial single-stranded annealing protein Mgm101
- MacMillan Mbantenkhu, S. Wierzbicki, Xiaowen Wang, Shangdong Guo, S. Wilkens, Xin Jie Chen
- Biology, ChemistryMolecular biology of the cell
- 15 May 2013
The C-tail of Mgm101 may couple ssDNA binding with ring disassembly, which facilitates the formation of nucleoprotein complexes competent for the repair of mtDNA.
Biochemical and functional characterization of Mgm101, a Rad52‐type recombination protein in mitochondria
- MacMillan Mbantenkhu, Xiowen Wang, J. Nardozzi, S. Wilkens, Xinchun Chen
- Biology
- 1 April 2012
The data support the idea that the Mgm101 C‐tail may represent a novel functional module for catalyzing DNA recombination, and show that the residues K253, W257, R259, Y268 and the triple mutant K251A‐K253A are critical for function.