Thomas Arthur Steitz, Ph.D
Dr. Thomas Steitz, a resident of Stony Creek and Yale professor, is a world class chemist who recently was awarded the Nobel Prize in Chemistry. I believe he should be considered as a candidate for induction into Branford's Education Hall of Fame.
Thomas Arthur Steitz, Ph.D., is a Sterling Professor of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University. Dr. Steitz was awarded the 2009 Nobel Prize in Chemistry along with Venkatraman Ramakrishnan and Ada Yonath "for studies of the structure and function of the ribosome". Dr. Steitz also won the Gairdner International Award in 2007 "for his studies on the structure and function of the ribosome which showed that the peptidyl transferase was an RNA catalyzed reaction, and for revealing the mechanism of inhibition of this function by antibiotics."
Dr. Steitz was born in Milwaukee, Wisconsin on August 23, 1940. He studied chemistry as an undergraduate at Lawrence University and received a Ph.D. in Biochemistry and Molecular Biology from Harvard University in 1966. He is married to Joan A. Steitz, also a Sterling Professor of Molecular Biophysics and Biochemistry at Yale. He lives in Stony Creek, CT.
The following article supports this letter of nomination. Yale's Thomas Steitz Shares 2009 Nobel Prize in Chemistry Described Structure and Function of Life's Protein-Making Factory
Thomas Arthur Steitz, Ph.D., is a Sterling Professor of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University. Dr. Steitz was awarded the 2009 Nobel Prize in Chemistry along with Venkatraman Ramakrishnan and Ada Yonath "for studies of the structure and function of the ribosome". Dr. Steitz also won the Gairdner International Award in 2007 "for his studies on the structure and function of the ribosome which showed that the peptidyl transferase was an RNA catalyzed reaction, and for revealing the mechanism of inhibition of this function by antibiotics."
Dr. Steitz was born in Milwaukee, Wisconsin on August 23, 1940. He studied chemistry as an undergraduate at Lawrence University and received a Ph.D. in Biochemistry and Molecular Biology from Harvard University in 1966. He is married to Joan A. Steitz, also a Sterling Professor of Molecular Biophysics and Biochemistry at Yale. He lives in Stony Creek, CT.
The following article supports this letter of nomination. Yale's Thomas Steitz Shares 2009 Nobel Prize in Chemistry Described Structure and Function of Life's Protein-Making Factory
Structure and function of biological macromolecules
Our general goal is to understand the biological functions of macromolecules in terms of their detailed molecular structure. Of particular interest are the molecular mechanisms by which those proteins and nucleic acids involved in the central dogma of molecular biology (DNA replication, transcription, translation and genetic recombination achieve their biological function. Virtually all aspects of the mainten rearrangement and expression of information stored ir the genome ir interactions between proteins and nucleic acids.
Our recent accomplishments have included the determination of the atomic structure of the 50S ribosomal subunit and its complexes with substrate, intermediate and product analogues as well as complexes with more than a dozen antibiotics. These structures establish that the is a ribozyme, provide insights into the mechanism of peptide bond formation and show how several classes of antibiotics function. In the of transcription, six structures of T7 RNA polymerase captured in various functional states show the structural basis of the transition from the initiation to elongation phase, which involves a large protein structure rearrangement. They explain the basis of promoter clearance, process of the elongation phase, translocation and strand separation. The stru of the CCA-adding enzyme captured in each state of CCA incorporated onto tRNA explain the enzyme's specificity for nucleotide incorporated the absence of a nucleic acid template. The structure of a recombination intermediate of y8 resolvase suggests that site specific recombination this enzyme is achieved by subunit rotation.
Future directions will focus on the complex macromolecular assembly that are the functional machines in these processes, including the ribc and the replisome. For example, we wish to establish the atomic structure of the ribosome captured in the act of protein synthesis in each of its conformational states with elongation factors as well as interacting w the proteins involved in protein secretion. Likewise, a mechanistic understanding of replication and recombination will require structure the assemblies in each step of their functioning. Hypotheses arising f1 these structures will be tested using site directed mutagenesis and biochemical studies to relate structure to function.
Our general goal is to understand the biological functions of macromolecules in terms of their detailed molecular structure. Of particular interest are the molecular mechanisms by which those proteins and nucleic acids involved in the central dogma of molecular biology (DNA replication, transcription, translation and genetic recombination achieve their biological function. Virtually all aspects of the mainten rearrangement and expression of information stored ir the genome ir interactions between proteins and nucleic acids.
Our recent accomplishments have included the determination of the atomic structure of the 50S ribosomal subunit and its complexes with substrate, intermediate and product analogues as well as complexes with more than a dozen antibiotics. These structures establish that the is a ribozyme, provide insights into the mechanism of peptide bond formation and show how several classes of antibiotics function. In the of transcription, six structures of T7 RNA polymerase captured in various functional states show the structural basis of the transition from the initiation to elongation phase, which involves a large protein structure rearrangement. They explain the basis of promoter clearance, process of the elongation phase, translocation and strand separation. The stru of the CCA-adding enzyme captured in each state of CCA incorporated onto tRNA explain the enzyme's specificity for nucleotide incorporated the absence of a nucleic acid template. The structure of a recombination intermediate of y8 resolvase suggests that site specific recombination this enzyme is achieved by subunit rotation.
Future directions will focus on the complex macromolecular assembly that are the functional machines in these processes, including the ribc and the replisome. For example, we wish to establish the atomic structure of the ribosome captured in the act of protein synthesis in each of its conformational states with elongation factors as well as interacting w the proteins involved in protein secretion. Likewise, a mechanistic understanding of replication and recombination will require structure the assemblies in each step of their functioning. Hypotheses arising f1 these structures will be tested using site directed mutagenesis and biochemical studies to relate structure to function.