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Human Physiology - Cell structure and function - EKU

Combined with the availability of highly purified, fluorescently labeled in vitro translation systems, the advent of single-molecule fluorescence imaging has ushered in a new era in high-resolution mechanistic studies of ribosome-catalyzed protein synthesis, or translation. Together with ensemble biochemical investigations of translation and structural studies of functional ribosomal complexes, in vitro single-molecule fluorescence imaging of protein synthesis is providing unique mechanistic insight into this fundamental biological process. More recently, rapidly evolving breakthroughs in fluorescence-based molecular imaging in live cells with sub-diffraction-limit spatial resolution and ever-increasing temporal resolution provide great promise for conducting mechanistic studies of translation and its regulation in living cells. Here we review the remarkable recent progress that has been made in these fields, highlight important mechanistic insights that have been gleaned from these studies thus far, and discuss what we envision lies ahead as these approaches continue to evolve and expand to address increasingly complex mechanistic and regulatory aspects of translation.

De novo synthesis the formation of an essential molecule from simple precursor molecules

They often require theexpenditure of energy to help compounds move across the membraneCells, cytoplasm, and : - controls cell function via transcriptionand translation (in other words, by controlling protein synthesis in acell)- DNA is used to produce mRNA- mRNA then moves from the nucleus into the cytoplasm & is usedto produce a protein

Internal ribosome entry site - Wikipedia

Background: DNA in our chromosomes is continuously exposed to chemical damage: from chemicals or radiation absorbed from the environment, but more commonly from byproducts of our own metabolism. The process of DNA replication is itself capable of damaging DNA. Our cells cope with DNA damage in a variety of ways, including direct reversal of the damage (e.g. re-connecting a broken DNA strand) and removal of chemically modified bases followed by re-synthesis of the proper DNA strand. Restoring the original DNA sequence often relies on information from an additional copy of the sequence: the opposite strand of the double helix (if undamaged) or a sister DNA molecule (if replication of that segment of DNA has already occurred).A common feature of many DNA repair processes is the separation and intertwining of DNA strands. This is assisted by enzymes called DNA helicases, which are essential participants in DNA repair and a variety of other processes. A number of human genetic disorders, including Bloom’s syndrome, Werner’s syndrome, Rothmund-Thomson syndrome and Xeroderma pigmentosum, result from defects in genes encoding DNA helicases. Each of these conditions has specific manifestations, but all share a high incidence of cancer, indicating the importance of DNA helicases to protection against cancer-causing mutations.An interesting twist on the role of the DNA repair machinery in cancer relates to the treatments used in cancer therapy. Radiotherapy and several modes of cancer chemotherapy rely on killing cancer cells through deliberate damage to the DNA. Paradoxically, powerful DNA repair mechanisms can help cancer cells evade the effects of chemotherapy. We clearly need to understand better the complex interactions between DNA repair pathways and survival of cancer cells in order to control these processes for therapeutic purposes.Project: This project focuses on a family of DNA helicases related to the RecQ protein; these include in the human RECQ1, Bloom, and Werner proteins, as well as RECQ4 and RECQ5. We aim to understand both the fundamental biochemistry of these proteins as well as exploring the medical potential of inhibiting one or more of these enzymes in cancer cells. At the basic level, we are analyzing the structures of helicases by X-ray crystallography, and using the structures as predictive tools to generate site –specific mutants and to guide the development of small-molecule inhibitors. At the medicinal chemistry level, we have developed the first cell-permeable inhibitors of BLM. This project will use structure-based and other methods to develop inhibitors with more favorable properties for use in more relvant cellular and in vivo models.Significance: We have developed the first inhibitors of DNA helicases, but this area has not been explored for its medical potential. This work is based on solid preliminary results, and will open an entirely new area of investigation with potential impact both on fundamental research and in future cancer therapy.

The ribosome is the universally conserved, two-subunit ribonucleoprotein ribozyme that synthesizes proteins by sequentially incorporating aminoacyl-transfer RNA (aa-tRNA) substrates in the order specified by the codon sequence of a messenger RNA (mRNA) template, a process termed translation () []. Over the past eight years, single-molecule fluorescence imaging has significantly expanded our mechanistic understanding of translation. We begin this article by briefly reviewing the prolific body of work that has emerged from single-molecule in vitro fluorescence studies of translation. Using a top-down approach, we open with a discussion of studies in which the overall rate of protein synthesis by single ribosomes has been measured and conclude with a synopsis of the numerous studies in which partial reactions within the translation pathway have been kinetically dissected with single-molecule resolution. We follow this by highlighting a number of exciting recent reports in which protein synthesis and ribosomes have been imaged in living cells using cutting-edge in vivo single-molecule fluorescence imaging approaches. Collectively, these advances in fluorescence imaging of translation are enabling researchers to address mechanistic questions that have remained difficult or impossible to address using ensemble biochemical approaches.

RCSB Protein Data Bank - RCSB PDB

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