CRISPR-Cas12a target binding unleashes indiscriminate single-stranded DNase activity
نویسندگان
چکیده
منابع مشابه
CRISPR-Cas12a-Assisted Recombineering in Bacteria
Clustered regularly interspaced short palindromic repeat (CRISPR)-Cas12a (Cpf1) has emerged as an effective genome editing tool in many organisms. Here, we developed and optimized a CRISPR-Cas12a-assisted recombineering system to facilitate genetic manipulation in bacteria. Using this system, point mutations, deletions, insertions, and gene replacements can be easily generated on the chromosome...
متن کاملSingle-stranded DNA-binding Proteins
The emergence of DNA as the predominant hereditary material of life has necessitated the evolution of proteins whose sole function is the maintenance and care of these vital molecules. In a typical cell, there is a wide array of proteins with specialized functions in DNA metabolism that allow the cell to maintain and replicate its genome. In order to copy or make repairs to DNA, the double heli...
متن کاملRNA-Independent DNA Cleavage Activities of Cas9 and Cas12a
CRISPR-Cas systems provide bacteria and archaea with sequence-specific protection against invading mobile genetic elements. In the presence of divalent metal ions, Cas9 and Cas12a (formerly Cpf1) proteins target and cleave DNA that is complementary to a cognate guide RNA. The recognition of a protospacer adjacent motif (PAM) sequence in the target DNA by Cas9 and Cas12a is essential for cleavag...
متن کاملRegulation of Gene Editing Activity Directed by Single-Stranded Oligonucleotides and CRISPR/Cas9 Systems
Single-stranded DNA oligonucleotides (ssODNs) can direct the repair of a single base mutation in human genes. While the regulation of this gene editing reaction has been partially elucidated, the low frequency with which repair occurs has hampered development toward clinical application. In this work a CRISPR/Cas9 complex is employed to induce double strand DNA breakage at specific sites surrou...
متن کاملBinding of the dimeric Deinococcus radiodurans single-stranded DNA binding protein to single-stranded DNA.
Deinococcus radiodurans single-stranded (ss) DNA binding protein (DrSSB) originates from a radiation-resistant bacterium and participates in DNA recombination, replication, and repair. Although it functions as a homodimer, it contains four DNA binding domains (OB-folds) and thus is structurally similar to the Escherichia coli SSB (EcoSSB) homotetramer. We examined the equilibrium binding of DrS...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Science
سال: 2018
ISSN: 0036-8075,1095-9203
DOI: 10.1126/science.aar6245