Recently discovered CRISPR enzyme from huge bacteriophages expands genome editing toolbox

July 16, 2020

A recently discovered hypercompact CRISPR enzyme found only in huge bacteriophages, and known as CRISPR-CasΦ, is functional, a new study by Patrick Pausch, Jennifer Doudna and colleagues reports, and it provides a powerful new tool in the CRISPR genome editing toolbox, including because it can target a wider range of genetic sequences compared to Cas9 and Cas12. The authors tested its target-expanding capabilities in human and plant cells. Given its small size, they also suggest CasΦ could offer novel advantages for cellular delivery relative to other CRISPR-Cas proteins. While commonly known as a tool for genetic engineering, in nature, CRISPR-Cas systems provide many single-celled organisms with an adaptive immunity against viruses and plasmids. CRISPR RNAs (crRNA) in the host recognize DNA in previously encountered viruses and direct CRISPR-associated or Cas enzymes to destroy the viruses. While CRISPR-Cas systems almost exclusively exist and operate in the genomes of bacteria and archaea, they've also recently been discovered in huge bacteriophages - the viruses of bacteria. However, these systems are different. They notably lack the Cas proteins commonly found in other CRISPR-Cas systems, yet exclusively harbor the genetically unique and unusually tiny CasΦ enzyme. Here, Pausch, Doudna and colleagues describe the functionality of the phage-derived CRISPR-CasΦ system and demonstrate its potential for expanding the CRISPR genome editing toolbox. Despite being nearly half the size of Cas9 and Cas12 systems commonly used for genome editing, Pausch et al. show that the biochemically unique CasΦ is fully functional and capable of both producing mature crRNA and cleaving the foreign DNA using only a single active site, making it the most compact CRISPR-Cas system yet identified. What's more, the authors demonstrate CasΦ's ability to be used successfully in both human and plant genome editing.

American Association for the Advancement of Science

Related Enzyme Articles from Brightsurf:

Repairing the photosynthetic enzyme Rubisco
Researchers at the Max Planck Institute of Biochemistry decipher the molecular mechanism of Rubisco Activase

Oldest enzyme in cellular respiration isolated
Researchers from Goethe University have found what is perhaps the oldest enzyme in cellular respiration.

UQ researchers solve a 50-year-old enzyme mystery
Advanced herbicides and treatments for infection may result from the unravelling of a 50-year-old mystery by University of Queensland researchers.

Overactive enzyme causes hereditary hypertension
After more than 40 years, several teams at the MDC and ECRC have now made a breakthrough discovery with the help of two animal models: they have proven that an altered gene encoding the enzyme PDE3A causes an inherited form of high blood pressure.

Triggered by light, a novel way to switch on an enzyme
In living cells, enzymes drive biochemical metabolic processes. It is this very ability which allows them to be used as catalysts in biotechnology, for example to create chemical products such as pharmaceutics.

A 'corset' for the enzyme structure
The structure of enzymes determines how they control vital processes such as digestion or immune response.

Could inhibiting the DPP4 enzyme help treat coronavirus?
Researchers and clinicians are scrambling to find ways to combat COVID-19, including new therapeutics and eventually a vaccine.

Bacterial enzyme could become a new target for antibiotics
Scientists discover the structure of an enzyme, found in the human gut, that breaks down a component of collagen.

Chemists create new artificial enzyme
Rajeev Prabhakar, a computational chemist at the University of Miami, and his collaborators at the University of Michigan have created a novel, synthetic, three-stranded molecule that functions just like a natural metalloenzyme, or an enzyme that contains metal ions.

First artificial enzyme created with two non-biological groups
Scientists at the University of Groningen turned a non-enzymatic protein into a new, artificial enzyme by adding two abiological catalytic components: an unnatural amino acid and a catalytic copper complex.

Read More: Enzyme News and Enzyme Current Events is a participant in the Amazon Services LLC Associates Program, an affiliate advertising program designed to provide a means for sites to earn advertising fees by advertising and linking to