Recombinant Proteins Quotes

Genes make proteins that regulate genes. Genes make proteins that replicate genes. The third R of the physiology of genes is a word that lies outside common human vocabulary, but is essential to the survival of our species: recombination—the ability to generate new combinations of genes.

You see, we—all of us—are alike at our core. From the lowest microorganism to the highest form of Sentient, we share the most basic aspects of all living things from protein folds to cellular organization. The secrets lie within the dual nature of intron and exon—expression and suppression and recombination of these—allowing life to seek infinite forms.

The cloning of human genes allowed scientists to manufacture proteins-and the synthesis of proteins opened the possibility of targeting the millions of biochemical reactions in the human body. Proteins made it possible for chemists to intervene on previously impenetrable aspects of our physiology. The use of recombinant DNA to produce proteins thus marked a transition not just between one gene and one medicine, but between genes and a novel universe of drugs.

Instead of the go-to ingredients previously used in animal protein substitutes — soy, wheat gluten, vegetable starches — Food 2.0 companies are using computer algorithms to analyze hundreds of thousands of plant species to find out what compounds can be stripped out and recombined to create what they say are more delicious and sustainable sources of protein.

The RAG [(Recombination-Activating Gene)] genes [which assist in the facilitation of V(D)J recombination] lack the introns that characterize eukaryotic genes. In this unusual feature they resemble the transposase gene of a transposon, a type of genetic element that can make and move copies of itself to different chromosomal locations. The essential components of a transposon are a transposase—an enzyme that cuts double-stranded DNA—and regions of repetitive DNA, called the terminal repeat sequences, that are recognized by the transposase. These two features allow the transposon to be excised from one location and inserted into another. The similarity of the RAG recombinase to a transposase has led to the hypothesis that the mechanism now used to rearrange immunoglobulin and T-cell receptor gene segments originated in a vertebrate ancestor with the insertion of a transposon into a gene encoding a receptor of innate immunity. The inserted transposase genes evolved to encode RAG proteins, and the terminal repeat sequences evolved to become the recombination signal sequences for the first rearranging gene segments. During this evolution, the transposase gene and the long terminal repeats of the transposon were separated and became components of different genes, both expressed specifically in lymphocytes. Today, the human RAG genes are on chromosome 11[,] and on four other chromosomes are the much-expanded sets of rearranging antigen-receptor genes.