Actin and tubulin synthesis essay - lifegeil-movement.com.
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Consequently, tubulin isolated from porcine brain tissue is highly homologous to tubulin isolated from any eukaryotic source. In biochemical terms, this fact results in the technical benefit that porcine tubulin (in the form of microtubules, see below) can be used to assay tubulin associated proteins originating from many diverse species, e.g.: yeast (1,2,3) and fruit fly (4,5).
Living polymerization of the two major proteins in eucaryotic cells: actin and tubulin is reviewed. Actin is a large globular protein built of 375 alpha-amino acid residues and has a molecular weight of 42,000.
The effect of lactate on synthesis of new proteins in isolated spermatids and spermatocytes of rats was examined. Lactate stimulated(35 S)methionine ((35 S)met) incorporation into both spermatids and spermatocytes.The rate of protein synthesis was positively correlated with the intracellular level of ATP.
It was thought that homologues of actin and tubulin (forming F-actin and microtubules in eukaryotes, respectively) are missing from all bacteria and archaea. In the past, we could show that FtsZ and MreB, present in a large number of bacteria, are clear homologues of eukaryotic tubulin and actin, respectively.
The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including bacteria and archaea. It extends from the cell nucleus to the cell membrane and is composed of similar proteins in the various organisms. In eukaryotes, it is composed of three main components, microfilaments, intermediate filaments and microtubules, and these are.
Three specific cytoskeletal proteins-- actin, vimentin, and tubulin--were synthesized at similar rates that were significantly slower than the average fractional synthesis rate for total protein. Myosin, on the other hand, was synthesized faster than average.