MBIB News

Ke Xu (left) and Wenjun Zhang (right) of the Biosciences Area have been named Alfred P. Sloan Foundation fellows. Xu is a faculty chemist in the Molecular Biophysics & Integrated Bioimaging Division and Zhang is a faculty biologist in the Environmental Genomics & Systems Biology Division. These scientists are two of the eight UC Berkeley assistant professors to be honored by the Foundation, along with 118 other new fellows announced today. Fellowships are awarded in eight scientific and technical fields: chemistry, computer science, economics, mathematics, computational and evolutionary molecular biology, neuroscience, ocean sciences and physics. Read more at Berkeley News.

Aymerick Eudes and Dominique Loqué of the Joint Bioenergy Institute (JBEI) led a study that shows for the first time that an enzyme can be tweaked to reduce lignin in plants. Their technique could help lower the cost of converting biomass into carbon-neutral fuels to power your car and other sustainably developed bio-products. The crystal structure of this enzyme was solved using data collected in the Berkeley Center for Structural Biology at the Advanced Light Source. Read more on the Berkeley Lab News Center.

In the latest round of intellectual property decisions from the US Patent & Trademark Office, Caribou Biosciences, co-founded by faculty scientist Jennifer Doudna, has been awarded intellectual property rights for CRISPR technology. The patent focuses on detecting areas in the genome that have been rearranged, versus genomic editing that would occur with the use of the associated Cas9 protein. CRISPR/Cas9 is a bacterial editing system that cuts and splices DNA sequences with unprecedented precision and speed and has become a technique used by scientists world-wide to study animal and plant cells. The patent dispute between the UC Regents and the Broad Institute was recently covered by the Los Angeles Times. More information about this recent decision can be found in The Daily Californian.

Two recently licensed vaccines against bacterial meningitis contain a bacterial surface protein antigen known as Factor H binding protein (FHbp). The native form of this protein can have low thermal stability, which limits its potential use as an antigen in vaccines. After engineering a more stable Factor H binding protein antigen, scientists from UC San Francisco Benioff Children’s Hospital Oakland determined the structure of the stabilized vaccine with the help of protein crystallography at the Advanced Light Source (ALS) in the Berkeley Center for Structural Biology (Beamline 5.0.1). Read more in the ALS Science Brief.

The CRISPR/Cas9 bacterial genomic editing system identifies and cleaves complementary target sequences in foreign DNA. CRISPR (clustered regularly interspaced short palindromic repeats)–associated (Cas) protein Cas9 begins its work by RNA-guided DNA unwinding to form an RNA-DNA hybrid and displacing a DNA strand inside the protein. Upon binding, Cas9 reorganizes into an R-loop complex that is necessary for it to perform its function. A recent article published in Science describes work done to uncover the structural basis of Cas9’s function.