Protein phosphorylation is a post-translational modification of proteins, was first reported in 1906 by which American biochemist who studied the structure and function of nucleic acids, at the Rockefeller Institute for Medical Research?
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Protein phosphorylation Protein phosphorylation is a post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or modifying its function. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. The amino acids most commonly phosphorylated are serine, threonine, and tyrosine in eukaryotes, and histidine in prokaryotes, which play important and well-characterized roles in signaling pathways and metabolism. However, many other amino acids can also be phosphorylated, including arginine, lysine, and cysteine. Protein phosphorylation was first reported in 1906 by Phoebus Levene at the Rockefeller Institute for Medical Research with the discovery of phosphorylated vitellin. However, it was nearly 50 years until the enzymatic phosphorylation of proteins by protein kinases was discovered.
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Phoebus Levene Phoebus Aaron Theodore Levene, M.D. (25 February 1869 – 6 September 1940) was an American biochemist who studied the structure and function of nucleic acids. He characterized the different forms of nucleic acid, DNA from RNA, and found that DNA contained adenine, guanine, thymine, cytosine, deoxyribose, and a phosphate group.
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Homer Smith Dr Homer William Smith (January 2, 1895 – March 25, 1962) was an American physiologist and an advocate for science, who spent most of his career at New York University School of Medicine. His research work focused on the kidney and he discovered inulin at the same time as A.N. Richards. Dr. Smith authored several books including "From Fish to Philosopher", "Man and His Gods", and "The Kidney: Structure and function in health and disease’'.
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Albert Claude Albert Claude (24 August 1899 – 22 May 1983) was a Belgian medical doctor and cell biologist who shared the Nobel Prize in Physiology or Medicine in 1974 with Christian de Duve and George Emil Palade. His elementary education started in a comprehensive primary school at Longlier, his birthplace. He served in the British Intelligence Service during the First World War, and got imprisoned in concentration camps twice. In recognition of his service, he was granted enrolment at the University of Liège in Belgium to study medicine without any formal education required for the course. He earned his Doctor of Medicine degree in 1928. Devoted to medical research, he initially joined German institutes in Berlin. In 1929 he found an opportunity to join the Rockefeller Institute in New York. At Rockefeller University he made his most groundbreaking achievements in cell biology. In 1930 he developed the technique of cell fractionation, by which he discovered the agent of the Rous sarcoma, components of cell organelles such as mitochondrion, chloroplast, endoplasmic reticulum, Golgi apparatus, ribosome and lysosome. He was the first to employ the electron microscope in the field of biology. In 1945 he published the first detailed structure of cell. His collective works established the complex functional and structural properties of cells.
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Histidine kinase Histidine kinases (HK) are multifunctional, and in non-animal kingdoms, typically transmembrane, proteins of the transferase class of enzymes that play a role in signal transduction across the cellular membrane. The vast majority of HKs are homodimers that exhibit autokinase, phosphotransfer, and phosphatase activity. HKs can act as cellular receptors for signaling molecules in a way analogous to tyrosine kinase receptors (RTK). Multifunctional receptor molecules such as HKs and RTKs typically have portions on the outside of the cell (extracellular domain) that bind to hormone- or growth factor-like molecules, portions that span the cell membrane (transmembrane domain), and portions within the cell (intracellular domain) that contain the enzymatic activity. In addition to kinase activity, the intracellular domains typically have regions that bind to a secondary effector molecule or complex of molecules that further propagate signal transduction within the cell. Distinct from other classes of protein kinases, HKs are usually parts of a two-component signal transduction mechanisms in which HK transfers a phosphate group from ATP to a histidine residue within the kinase, and then to an aspartate residue on the receiver domain of a response regulator protein (or sometimes on the kinase itself). More recently, the widespread existence of protein histidine phosphorylation distinct from that of two-component histidine kinases has been recognised in human cells. It is worth noting that, in marked contrast to Ser, Thr and Tyr phosphorylation, the analysis of phosphorylated Histidine using standard biochemical and mass spectrometric approaches is much more challenging.
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Philip Siekevitz Philip Siekevitz (1918-2009) was an American cell biologist who spent most of his career at Rockefeller University. He was involved in early studies of protein synthesis and trafficking, established purification techniques to facilitate study of the cell nucleus, worked with Nobel Prize in Physiology or Medicine winner George Palade on cell membrane dynamics, and published extensively on the subject of postsynaptic density.
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Phosphatome The phosphatome of an organism is the set of phosphatase genes in its genome. Phosphatases are enzymes that catalyze the removal of phosphate from biomolecules. Over half of all cellular proteins are modified by phosphorylation which typically controls their functions. Protein phosphorylation is controlled by the opposing actions of protein phosphatases and protein kinases.
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Gerald Penn Gerald Penn is a clinical immunologist, and a pioneer in the field of clinical immunoelectrophoresis. He was a student of Henry Kunkel at Rockefeller University from 1968 to 1970, and holds both an M.D. and Ph.D. from the Ohio State University. His research also includes one of the earliest studies on the negative effects of naturally occurring stressors on the response of the human immune system. He is a clinical associate professor of pathology at the Ohio State University.
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Ruby Hirose Ruby Sakae Hirose (1904 – 1960) was an American biochemist and bacteriologist. She did research on blood clotting and Thrombin, allergies, and researched cancer using antimetabolites.
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Evgeny Nudler Evgeny Nudler is an American biochemist, currently the Julie Wilson Anderson Professor at New York University School of Medicine.
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Histone code The histone code is a hypothesis that the transcription of genetic information encoded in DNA is in part regulated by chemical modifications to histone proteins, primarily on their unstructured ends. Together with similar modifications such as DNA methylation it is part of the epigenetic code. Histones associate with DNA to form nucleosomes, which themselves bundle to form chromatin fibers, which in turn make up the more familiar chromosome. Histones are globular proteins with a flexible N-terminus (taken to be the tail) that protrudes from the nucleosome. Many of the histone tail modifications correlate very well to chromatin structure and both histone modification state and chromatin structure correlate well to gene expression levels. The critical concept of the histone code hypothesis is that the histone modifications serve to recruit other proteins by specific recognition of the modified histone via protein domains specialized for such purposes, rather than through simply stabilizing or destabilizing the interaction between histone and the underlying DNA. These recruited proteins then act to alter chromatin structure actively or to promote transcription.
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Protein structure Protein structure is the three-dimensional arrangement of atoms in a protein molecule. Proteins are polymers — specifically polypeptides — formed from sequences of amino acids, the monomers of the polymer. A single amino acid monomer may also be called a residue indicating a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, and dual polarisation interferometry to determine the structure of proteins.
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Bruce Ames Bruce Nathan Ames (born December 16, 1928) is an American biochemist. He is a professor of Biochemistry and Molecular Biology Emeritus at the University of California, Berkeley, and a senior scientist at Children's Hospital Oakland Research Institute (CHORI). He is the inventor of the Ames test, a system for easily and cheaply testing the mutagenicity of compounds.
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Wendell Meredith Stanley Wendell Meredith Stanley (16 August 1904 – 15 June 1971) was an American biochemist, virologist and Nobel laureate.
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Mark Rasenick Mark Rasenick is an American biologist, focusing on G protein signaling in the nervous system and the relationship of neurotransmitter activation to rapid modification of the cytoskeleton and how G proteins and the cytoskeleton work in concert to modify synaptic shape and to form a molecular basis for depression and the action of antidepressant drugs, at University of Illinois and an Elected Fellow of the American Association for the Advancement of Science. He has significant contributions towards advancing the understanding of neurotransmitter signaling and the biology of mood disorders and his research helped identify a membrane protein, the localization of which can be used as a biomarker for depression.
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Protein Science Protein Science is a peer-reviewed scientific journal covering research on the structure, function, and biochemical significance of proteins, their role in molecular and cell biology, genetics, and evolution, and their regulation and mechanisms of action. It is published by Wiley-Blackwell on behalf of The Protein Society.
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Joseph Schlessinger Joseph Schlessinger (born Josip Schlessinger; 26 March 1945) is a Yugoslav-born Israeli-American biochemist and biophysician. He is chair of the Pharmacology Department at Yale University School of Medicine in New Haven, Connecticut, as well as the founding director of the school's new Cancer Biology Institute. His area of research is signaling through tyrosine phosphorylation, which is important in many areas of cellular regulation, especially growth control and cancer. Schlessinger's work has led to an understanding of the mechanism of transmembrane signaling by receptor tyrosine kinases and how the resulting signals control cell growth and differentiation.
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Nucleoplasmin Nucleoplasmin, the first identified molecular chaperone is a thermostable acidic protein with a pentameric structure. The protein was first isolated from Xenopus species
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Aaron Novick Aaron Novick (June 24, 1919 – December 21, 2000) is considered one of the founders of molecular biology. He started the University of Oregon's Institute of Molecular Biology, believed to be the first of its kind in the world, in 1959.
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Bruce Alberts Bruce Michael Alberts (born April 14, 1938 in Chicago, Illinois) is an American biochemist and the Chancellor’s Leadership Chair in Biochemistry and Biophysics for Science and Education at the University of California, San Francisco. He has done important work studying the protein complexes which enable chromosome replication when living cells divide. He is known as an original author of the "canonical, influential, and best-selling scientific textbook" "Molecular Biology of the Cell", and as Editor-in-Chief of "Science" magazine.
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Signal transduction Signal transduction is the process by which a chemical or physical signal is transmitted through a cell as a series of molecular events, most commonly protein phosphorylation catalysed by protein kinases, which ultimately results in a cellular response. Proteins responsible for detecting stimuli are generally termed receptors, although in some cases the term sensor is used. The changes elicited by ligand binding (or signal sensing) in a receptor give rise to a signaling cascade, which is a chain of biochemical events along a signaling pathway. When signaling pathways interact with one another they form networks, which allow cellular responses to be coordinated, often by combinatorial signaling events. At the molecular level, such responses include changes in the transcription or translation of genes, and post-translational and conformational changes in proteins, as well as changes in their location. These molecular events are the basic mechanisms controlling cell growth, proliferation, metabolism and many other processes. In multicellular organisms, signal transduction pathways have evolved to regulate cell communication in a wide variety of ways.
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Erwin Chargaff Erwin Chargaff (11 August 1905 – 20 June 2002) was an Austro-Hungarian biochemist that immigrated to the United States during the Nazi era and was a professor of biochemistry at Columbia University medical school. Through careful experimentation, Chargaff discovered two rules that helped lead to the discovery of the double helix structure of DNA.