R
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
The Molecular Basis of N-End Rule Recognition
TL;DR: It is shown that mutation of critical ClpS contact residues abrogates substrate delivery to and degradation by the AAA+ protease ClpAP, and it is demonstrated that modification of the hydrophobic pocket results in altered N-end rule specificity, and functional implications for the mechanism of substrate delivery are discussed.
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An evolutionary bridge to a new protein fold.
TL;DR: Here, Arc-N11L is shown to be able to adopt either the wild type or mutant conformations, and serves as an evolutionary bridge from the β-sheet to the helical fold.
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Identification of Active Site Residues of the Tsp Protease
TL;DR: Alanine substitutions at three positions, Ser-430, Asp-441, and Lys-455, result in inactive proteases that have structures and substrate-binding properties similar to wild type, suggesting that the side chains at these positions participate in catalysis.
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Direct and adaptor-mediated substrate recognition by an essential AAA+ protease
TL;DR: A biochemical framework is established to understand regulated proteolysis in C. crescentus and it is suggested that cell-cycle regulation of CtrA stability depends on repression of its intrinsic degradation rather than adaptor-mediated enhancement.
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Purification and properties of alanine tRNA synthetase from Escherichia coli A tetramer of identical subunits.
TL;DR: The enzyme was proven to be an alpha 4 tetramer with a Mr = 380,000 by the following criteria and, in contrast to the native enzyme, oligomerization of the fragment could be not detected either by gel filtration chromatography or by dimethyl suberimidate cross-linking.