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Robert T. Sauer
Researcher at Massachusetts Institute of Technology
Publications - 408
Citations - 42127
Robert T. Sauer is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Repressor & Protein degradation. The author has an hindex of 106, co-authored 402 publications receiving 40181 citations. Previous affiliations of Robert T. Sauer include University of California, San Francisco & Harvard University.
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Journal ArticleDOI
Nickel coordination is regulated by the DNA-bound state of NikR
PE Carrington,Peter T. Chivers,Peter T. Chivers,Faizah Al-Mjeni,Faizah Al-Mjeni,Robert T. Sauer,Michael J. Maroney +6 more
TL;DR: The structure of the high-affinity nickel-binding site in NikR is reported and it is shown that it responds dramatically to DNA binding, an unanticipated feature of the NikR structure.
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Stable, monomeric variants of lambda Cro obtained by insertion of a designed beta-hairpin sequence
TL;DR: A Cro variant was designed and constructed in which the antiparallel beta-ribbon that forms the dimer interface was replaced by a beta-hairpin, and the engineered monomer has a folded structure similar to wild type, is significantly more stable than wildtype, and exhibits novel half-operator binding activity.
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Restriction of the Conformational Dynamics of the Cyclic Acyldepsipeptide Antibiotics Improves Their Antibacterial Activity
TL;DR: It is shown that the rigidified ADEP analogs bind and activate ClpP at lower concentrations in vitro and have up to 1200-fold enhanced antibacterial activity when compared to those with the peptidolactone core structure common to two ADEP natural products.
Journal ArticleDOI
C-terminal specific protein degradation: activity and substrate specificity of the Tsp protease.
Kenneth C. Keiler,Karen R. Silber,Kevin M. Downard,Ioannis A. Papayannopoulos,Klaus Biemann,Robert T. Sauer +5 more
TL;DR: Tsp displays a preference for substrates that are not stably folded: unstable variants of Arc repressor are better substrates than a hyperstable mutant, and a peptide with little stable structure is cleaved more efficiently than a protein substrate.
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Isolation and analysis of arc repressor mutants: evidence for an unusual mechanism of DNA binding.
TL;DR: It is argued that these N‐terminal residues are important for operator recognition but that they are not part of a conventional helix‐turn‐helix DNA binding structure and that Arc may use a new mechanism for sequence specific DNA binding.