Professor, Department of Biochemistry and Molecular Biology
Research Summary
The central interests of the Zimmermann laboratory are focused on the structure, function and evolution of ribosomes, the organelles that carry out protein synthesis in all living cells.
The long-term goal of our research is to obtain a detailed description of ligand-ribosome interactions during peptide bond formation and to explore the hypothesis that the ribosome is a dynamic entity whose moving parts promote translation. Although recent high-resolution cryo-EM and crystallographic images provide new insights into the mechanism of translation, these 'snapshots' do not explain how the ribosome interacts with its ligands or how structural changes in the ribosome facilitate this process. Our specific objectives are to define the structural and functional relationships between tRNA and the components of the peptidyl transferase center (PTC) and the exit site (E site) of the E. coli 50S ribosomal subunit, using chemical, biochemical and genetic approaches.
We are presently examining putative differences in the structural organization of the PTC of archaeal and (eu)bacterial ribosomes, as well as possible changes in the position of tRNA relative to 23S rRNA during peptidyl transfer, by qualitative and quantitative analysis of the pattern of short-range, photochemically-induced crosslinks to the PTC from the 3' nucleotide of tRNA at the P and A sites and a transition-state analog that spans both.
Crystallography and tRNA crosslinking have revealed that there is a protein, L27, at or near the PTC of the (eu)bacterial 50S ribosomal subunit, a region that is otherwise composed entirely of RNA. Moreover, deletion of L27 leads to severe defects in translation. We are assessing the functional role of L27 by investigating the effects of specific mutations on cell growth and ribosome activity.
Protein L1 and its associated RNA comprise a flexible and semi-autonomous domain within the 50S subunit that appears to promote the release of deacyated tRNA from the ribosome following peptide bond formation. To test this theory, we are investigating the ability of tRNA to interact with L1-RNA fragment complexes in vitro and the effects of specific mutations in L1 and the adjacent portions of the 23S rRNA on tRNA release in vivo.
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The central interests of the Zimmermann laboratory are focused on the structure, function and evolution of ribosomes, the organelles that carry out protein synthesis in all living cells.
The long-term goal of our research is to obtain a detailed description of ligand-ribosome interactions during peptide bond formation and to explore the hypothesis that the ribosome is a dynamic entity whose moving parts promote translation. Although recent high-resolution cryo-EM and crystallographic images provide new insights into the mechanism of translation, these 'snapshots' do not explain how the ribosome interacts with its ligands or how structural changes in the ribosome facilitate this process. Our specific objectives are to define the structural and functional relationships between tRNA and the components of the peptidyl transferase center (PTC) and the exit site (E site) of the E. coli 50S ribosomal subunit, using chemical, biochemical and genetic approaches.
We are presently examining putative differences in the structural organization of the PTC of archaeal and (eu)bacterial ribosomes, as well as possible changes in the position of tRNA relative to 23S rRNA during peptidyl transfer, by qualitative and quantitative analysis of the pattern of short-range, photochemically-induced crosslinks to the PTC from the 3' nucleotide of tRNA at the P and A sites and a transition-state analog that spans both.
Crystallography and tRNA crosslinking have revealed that there is a protein, L27, at or near the PTC of the (eu)bacterial 50S ribosomal subunit, a region that is otherwise composed entirely of RNA. Moreover, deletion of L27 leads to severe defects in translation. We are assessing the functional role of L27 by investigating the effects of specific mutations on cell growth and ribosome activity.
Protein L1 and its associated RNA comprise a flexible and semi-autonomous domain within the 50S subunit that appears to promote the release of deacyated tRNA from the ribosome following peptide bond formation. To test this theory, we are investigating the ability of tRNA to interact with L1-RNA fragment complexes in vitro and the effects of specific mutations in L1 and the adjacent portions of the 23S rRNA on tRNA release in vivo.
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About Robert A. Zimmermann
Research Summary
The central interests of the Zimmermann laboratory are focused on the structure, function and evolution of ribosomes, the organelles that carry out protein synthesis in all living cells.
The long-term goal of our research is to obtain a detailed description of ligand-ribosome interactions during peptide bond formation and to explore the hypothesis that the ribosome is a dynamic entity whose moving parts promote translation. Although recent high-resolution cryo-EM and crystallographic images provide new insights into the mechanism of translation, these 'snapshots' do not explain how the ribosome interacts with its ligands or how structural changes in the ribosome facilitate this process. Our specific objectives are to define the structural and functional relationships between tRNA and the components of the peptidyl transferase center (PTC) and the exit site (E site) of the E. coli 50S ribosomal subunit, using chemical, biochemical and genetic approaches.
We are presently examining putative differences in the structural organization of the PTC of archaeal and (eu)bacterial ribosomes, as well as possible changes in the position of tRNA relative to 23S rRNA during peptidyl transfer, by qualitative and quantitative analysis of the pattern of short-range, photochemically-induced crosslinks to the PTC from the 3' nucleotide of tRNA at the P and A sites and a transition-state analog that spans both.
Crystallography and tRNA crosslinking have revealed that there is a protein, L27, at or near the PTC of the (eu)bacterial 50S ribosomal subunit, a region that is otherwise composed entirely of RNA. Moreover, deletion of L27 leads to severe defects in translation. We are assessing the functional role of L27 by investigating the effects of specific mutations on cell growth and ribosome activity.
Protein L1 and its associated RNA comprise a flexible and semi-autonomous domain within the 50S subunit that appears to promote the release of deacyated tRNA from the ribosome following peptide bond formation. To test this theory, we are investigating the ability of tRNA to interact with L1-RNA fragment complexes in vitro and the effects of specific mutations in L1 and the adjacent portions of the 23S rRNA on tRNA release in vivo.
The central interests of the Zimmermann laboratory are focused on the structure, function and evolution of ribosomes, the organelles that carry out protein synthesis in all living cells.
The long-term goal of our research is to obtain a detailed description of ligand-ribosome interactions during peptide bond formation and to explore the hypothesis that the ribosome is a dynamic entity whose moving parts promote translation. Although recent high-resolution cryo-EM and crystallographic images provide new insights into the mechanism of translation, these 'snapshots' do not explain how the ribosome interacts with its ligands or how structural changes in the ribosome facilitate this process. Our specific objectives are to define the structural and functional relationships between tRNA and the components of the peptidyl transferase center (PTC) and the exit site (E site) of the E. coli 50S ribosomal subunit, using chemical, biochemical and genetic approaches.
We are presently examining putative differences in the structural organization of the PTC of archaeal and (eu)bacterial ribosomes, as well as possible changes in the position of tRNA relative to 23S rRNA during peptidyl transfer, by qualitative and quantitative analysis of the pattern of short-range, photochemically-induced crosslinks to the PTC from the 3' nucleotide of tRNA at the P and A sites and a transition-state analog that spans both.
Crystallography and tRNA crosslinking have revealed that there is a protein, L27, at or near the PTC of the (eu)bacterial 50S ribosomal subunit, a region that is otherwise composed entirely of RNA. Moreover, deletion of L27 leads to severe defects in translation. We are assessing the functional role of L27 by investigating the effects of specific mutations on cell growth and ribosome activity.
Protein L1 and its associated RNA comprise a flexible and semi-autonomous domain within the 50S subunit that appears to promote the release of deacyated tRNA from the ribosome following peptide bond formation. To test this theory, we are investigating the ability of tRNA to interact with L1-RNA fragment complexes in vitro and the effects of specific mutations in L1 and the adjacent portions of the 23S rRNA on tRNA release in vivo.
| Present | Professor, Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst | |
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Research Interests
Contact Information
Lederle Grad Research Tower, Rm 922
University of Massachusetts Amherst
Amherst, MA. 01003
Tel:413-545-0936
Email:
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