Protein Secretion - Structural basis for signal sequence recognition
Recognition of signal sequences by cognate receptors is a decisive step in correctly sorting secretory from nonsecretory proteins. We have determined the solution structure of a secretion signal sequence in complex with an essential bacterial receptor, SecA, the 204-kDa ATPase motor of the Sec translocase machinery.
The combined data not only explain how SecA may achieve the promiscuous recognition of a large set of signal sequences, but also provide insight into how the Sec nanomachinery may ultimately be assembled. These results are now published in Cell.
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Rated as "Exceptional" by Faculty 1000
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Signal Transduction - Control by proline isomerization
We have shown that autoinhibition can be controlled by an intrinsic intramolecular switch afforded by prolyl cis-trans isomerization. Peptidyl-prolyl isomerase enzymes such as cyclophilin A accelerate the slow cis-trans intervonversion rate. Proline isomerization appears to make an ideal switch that can regulate the kinetics of activation, thereby modulating the dynamics of signal response. These results are now published in Molecular Cell.
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Linda Nicholson & Kun Ping Lu wrote a nice Preview entitled "Prolyl cis-trans isomerization as a molecular timer in Crk signaling"
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Protein Allostery - It can be dynamically mediated!
We have shown that allosteric interactions can be mediated exclusively by transmitted changes in protein motions, in the absence of conformational changes.
Our results provide strong support of the existence of purely dynamics-driven allostery. These data are now published in Nature Structural & Molecular Biology.
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Lewis Kay discussed our paper in the "Journal Club" of Nature; he writes that "The molecular dance of a protein allows a chemist's secret wish to come true"
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Protein Secretion - SecA motor properties
SecA is an exquisitely designed and engineered protein motor that recognizes secretory proteins and couples their transport through the transmembrane SecYEG channel to ATP binding and hydrolysis.
Using an integrated NMR, thermodynamic, and biochemical approach
we have discovered a novel mechanism that underlies its function.
The results are published in Nature Structural & Molecular Biology (article of the month).
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John Hunt and coworkers wrote a nice News & Views entitled "Disorder breathes life into a DEAD motor"
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Transcription Regulation - Structural basis
Sequence-specific protein-DNA interactions are responsible for the
regulation of key biological functions such as replication of the
genome, initiation of transcription, and repair of damaged DNA.
We have recently provided the structural and dynamic basis of the
complete recognition pathway of the lac repressor system. The results
have been published in Science.
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Peter von Hippel wrote a nice Perspective entitled "Completing the view of transcriptional regulation"
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