AI Article Synopsis
- The maintenance of mitochondrial DNA (mtDNA) relies on various nuclear-encoded proteins, including the essential mtDNA helicase that aids in DNA replication.
- The human mtDNA helicase resembles the T7 bacteriophage primase-helicase and functions by unwinding DNA in a specific direction.
- This text discusses methods to identify the oligomeric state of the mtDNA helicase and examine its modular structure, emphasizing the practical use of these techniques for studying similar oligomeric proteins.
Article Abstract
Maintenance of the mitochondrial DNA (mtDNA) genome is dependent on numerous nuclear-encoded proteins including the mtDNA helicase, which is an essential component of the replicative machinery. Human mtDNA helicase shares a high degree of sequence similarity with the bacteriophage T7 primase-helicase gene 4 protein, and catalyzes duplex unwinding in the 5'-3' direction. As purified at 300 mM NaCl, the enzyme exists as a hexamer, with a modular architecture comprising distinct N- and C-terminal domains. We present here several methods that allow the identification of the oligomeric state of the human mtDNA helicase, and probe the modular architecture of the enzyme. Despite their relatively common usage, we believe that their versatility makes these techniques particularly helpful in the characterization of oligomeric proteins.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3312032 | PMC |
| http://dx.doi.org/10.1016/j.ymeth.2010.03.005 | DOI Listing |
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