
How are restriction enzymes used to make both recombinant DNA and transgenic organisms?
Answer
543.9k+ views
Hint: An enzyme that cuts or cleaves DNA into fragments at or close particular recognition sites inside molecules known as restriction sites is a restriction enzyme, restriction endonuclease. Restriction enzymes are one class of the larger enzyme category of endonucleases.
Complete answer:
Relevant DNA sites were cut by the restriction enzymes and helped to introduce the genes into transgenic animals. The restriction enzymes in a particular series have the property of cleaving DNA molecules. These restriction enzymes are used to sever sequences of DNA at particular nucleotide sites. To make recombinant DNA, such foreign genes are inserted into plasmids. The engineered plasmids are injected into bacteria for creating transgenic species.
Restriction enzyme type I, known to spontaneously cleave DNA away from the site of recognition, were the restriction enzymes studied by Arber and Meselson. The first type II restriction enzyme, Hind II, was isolated and characterized from the Haemophilus influenzae bacterium in 1970 by Hamilton O. Smith, Thomas Kelly, and Kent Wilcox. For laboratory work, restriction enzymes of this form are more effective as they cleave DNA at the site of their recognition sequence and are more commonly used as a molecular biology instrument.
Note: Restriction enzymes possibly developed from a shared ancestor and became universal by horizontal transmission of genes. Additionally, there is growing proof that endonuclease restriction has evolved as a selfish genetic feature .
Complete answer:
Relevant DNA sites were cut by the restriction enzymes and helped to introduce the genes into transgenic animals. The restriction enzymes in a particular series have the property of cleaving DNA molecules. These restriction enzymes are used to sever sequences of DNA at particular nucleotide sites. To make recombinant DNA, such foreign genes are inserted into plasmids. The engineered plasmids are injected into bacteria for creating transgenic species.
Restriction enzyme type I, known to spontaneously cleave DNA away from the site of recognition, were the restriction enzymes studied by Arber and Meselson. The first type II restriction enzyme, Hind II, was isolated and characterized from the Haemophilus influenzae bacterium in 1970 by Hamilton O. Smith, Thomas Kelly, and Kent Wilcox. For laboratory work, restriction enzymes of this form are more effective as they cleave DNA at the site of their recognition sequence and are more commonly used as a molecular biology instrument.
Note: Restriction enzymes possibly developed from a shared ancestor and became universal by horizontal transmission of genes. Additionally, there is growing proof that endonuclease restriction has evolved as a selfish genetic feature .
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