Tag Archives: Seth Darst

Atomic-scale view of bacterial proteins offers path to new tuberculosis drugs

New molecular insights are giving scientists ideas for how to combat antibiotic-resistant strains
In studying a cousin of the bacterium that causes tuberculosis, scientists have drawn a molecular map of the target for rifampicin, a common antibiotic. They are now using it in an effort to combat multi-resistant tuberculosis, for which existing treatments don’t work. More »

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Studies describe key role for a protein in cell division

New research shows how one protein, PRC1, acts in the penultimate stage of cell division to help form the architectural structures, called central spindles, needed before the cell can split in two. More »

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Rifamycin antibiotics attack tuberculosis bacteria with walls, not signals

When it comes to describing how a potent class of antibiotics kills deadly tuberculosis-causing bacteria, the more beautiful model is not always the right one. New research shows that a simple physical barrier rather than a complex allosteric mechanism still best explains how these antibiotics keep the bacteria in check — and how they fight back. More »

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Seth Darst joins National Academy of Sciences

Seth Darst, whose research explores the mechanisms by which RNA is transcribed from DNA, has been elected to the National Academy of Sciences, one of the highest honors given to a scientist or engineer in the United States. More »

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Newly solved structure reveal how cells resist oxygen damage

Cells have evolved multiple lines of defense to protect themselves from the effects of singlet oxygen, a toxic byproduct of photosynthesis. After five years of study, Rockefeller University researchers have become the first to solve the structure of a protein complex that regulates this process, using a zinc ion to quench singlet oxygen’s harmful properties. More »


Structure shows how a key protein in gene activation is controlled

Using the structure of the protein σ28 bound to its inhibitor as inspiration, a new structural study finds that this gene activator can also inhibit itself from binding to and expressing the wrong gene at the wrong time. More »

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Modular structure enables TRCF protein to both halt transcription and repair DNA

Using x-ray crystallography, Rockefeller scientists have now solved the structure of a protein — called Transcription-Repair Coupling Factor or TRCF — that plays a dual role in DNA transcription repair. The results show that TRCF employs a modular structure which would allow for conformational changes so that TRCF’s recruitment of the repair machinery doesn’t interfere with its interruption of transcription. More »

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Three-D images shed light on first steps of RNA synthesis

The first three-dimensional images of the initiating form of the molecular machinery in bacteria that “transcribes” genetic information from DNA into RNA — the crucial first step for making proteins — is reported in a pair of papers in the May 17 issue of the journal Science. More »

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Rockefeller Researchers Produce 3-D Picture of DNA-reading Molecular Machine

Researchers at The Rockefeller University have determined the first three-dimensional structure of the cellular RNA polymerase (RNAP), a molecular machine that activates individual genes by transcribing, or reading out, the instructions encoded in their DNA. The structure, published in the Sept. 17 issue of the journal Cell, provides scientists with a model for understanding the RNAPs of higher organisms, including humans. More »

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