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Full-Text Articles in Molecular Biology
Structure And Mechanism Of Mycobacterial Topoisomerase I, Nan Cao
Structure And Mechanism Of Mycobacterial Topoisomerase I, Nan Cao
FIU Electronic Theses and Dissertations
The enzyme DNA topoisomerase I is an essential enzyme that plays an important role in eukaryotic and prokaryotic cellular processes such as DNA replication, transcription, recombination and repair. Mycobacterium tuberculosistopoisomerase I (MtTOP1) is a validated drug target for antituberculosis treatment. Mycobacterial topoisomerase I regulates the topological constraints in chromosomes and helps in maintaining the growth of mycobacteria. The N- terminal domain (NTD) of mycobacterial topoisomerase I contains conserved catalytic domains that along with the active site Tyrosine are involved in cleaving and rejoining a single strand of DNA. Magnesium is required in DNA cleavage activity of type IA topoisomerases. …
A Multisession, Undergraduate Molecular Biology Lab Experiment Using Green Fluorescent Protein Including Subcloning And Color Changing Mutagenesis, Nathan S. Winter
A Multisession, Undergraduate Molecular Biology Lab Experiment Using Green Fluorescent Protein Including Subcloning And Color Changing Mutagenesis, Nathan S. Winter
Chemistry Faculty Publications
This paper describes a series of experiments involving handling and manipulating the DNA coding for Green Fluorescent Protein (GFP) including the subcloning of this gene, and mutating the DNA so that Cyan Fluorescent Protein (CFP) or Blue Fluorescent protein (BFP) are expressed. The primers needed for the PCR based subcloning of GFP are presented, as are those needed to mutate the GFP to either CFP or BFP.