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Rolling circle replication (RCR) is a process of unidirectional nucleic acid replication that can rapidly synthesize multiple copies of circular molecules of DNA or RNA, such as plasmids, the genomes of bacteriophages, and the circular RNA genome of viroids. Some eukaryotic viruses also replicate their DNA or RNA via the rolling circle mechanism.
A rolling circle mechanism that produces linear strands while progressing in a loop around the circular genome is also common. [8] Some dsDNA viruses use a strand displacement method whereby one strand is synthesized from a template strand, and a complementary strand is then synthesized from the prior synthesized strand, forming a dsDNA genome. [9]
Orthopoxvirus particles. A DNA virus is a virus that has a genome made of deoxyribonucleic acid (DNA) that is replicated by a DNA polymerase.They can be divided between those that have two strands of DNA in their genome, called double-stranded DNA (dsDNA) viruses, and those that have one strand of DNA in their genome, called single-stranded DNA (ssDNA) viruses. dsDNA viruses primarily belong ...
The circular fragments are copied by rolling circle replication resulting in many single-stranded copies of each fragment. The DNA copies concatenate head to tail in a long strand, and are compacted into a DNA nanoball. The nanoballs are then adsorbed onto a sequencing flow cell.
The observed DNA replication intermediates included circular and branched circular concatemeric structures that likely arose by rolling circle replication. When assembling concatemers from synthetic oligonucleotides, increasing salt concentration to 200 mM was found to be a major optimizing factor due to its ability to enhance ionic strength ...
PcrA, standing for plasmid copy reduced is a helicase that was originally discovered in a screen for chromosomally encoded genes that are affected in plasmid rolling circle replication in the Gram-positive pathogen Staphylococcus aureus.
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The polymerase is a monomeric protein with two distinct functional domains. Site-directed mutagenesis experiments support the proposition that this protein displays a structural and functional similarity to the Klenow fragment of the Escherichia coli Polymerase I enzyme; [3] it comprises a C-terminal polymerase domain and a spatially separated N-terminal domain with a 3'-5' exonuclease activity.