Recently, Professor Yan Ning from Tsinghua University, Tsinghua University-Peking University Life Science Joint Center published an article entitled "Revisiting the TALE repeat", which put forward new views on this protein repeat structure, which will help to understand TALE in depth Protein, and promote the affinity and specificity of TALEN technology design.

TALE is a protein injected into the host cell by the plant pathogenic bacteria Xanthomonas through the type III secretion system. The peculiarity of TALE protein is its DNA binding domain-this DNA binding domain is different from other known DNA binding domains. It consists of different numbers of repeating units, and each repeating unit specifically recognizes a DNA base pair.

In most cases, each repeat unit consists of 34 amino acids. Among these 34 amino acids, except for the amino acid changes at positions 12 and 13, the other amino acids are highly conservative. These two non-conservative amino acids are named RVD (repeat variable diresidue). There is a special one-to-one correspondence between the 12 and 13 amino acids in each repeat sequence and the recognized nucleotide type.

The specific DNA sequence recognition and flexible assembly of TALE proteins provide great prospects for their application in molecular biology. Scientists can design and assemble any TALE unit to recognize the target DNA double helix sequence. This feature has been used to construct the DNase TALEN (TALE nuclease) that cleaves specific double-stranded DNA sequences, and has been successfully used to introduce site-directed mutations and site-directed knockouts into cell genomes.

In 2012, Professor Yan Ning, in collaboration with Professor Shi Yigong and Professor Zhu Jianjian, reported on the molecular mechanism of the transcriptional activator-like effector protein TALE specifically recognizing DNA. Since then, they have discovered that TALE can specifically recognize DNA-RNA hybrid strands and protect DNA-RNA hybrid strands are not degraded by nucleases.

On the basis of these studies, Professor Yan Ning ’s research group proposed a structure-based TALE repeat sequence redistribution. This new numbering system unifies the family of TALE and the α-spiral superfamily and reflects the TAL effect. The structural integrity of the factor.

In addition, the researchers also analyzed the crystal structure of the dHax3 mutation in the complex of 15 target DNA molecules, which explained the structural basis for the recognition of adenine (A) and guanine (G). These structural analyses are helpful to deepen our understanding of TALE protein and improve the affinity and specificity in TALEN technology design.

Professor Yan Ning also published a review before, introducing a special transport protein-proton-coupled secondary transport protein, which is widely present in the body's nutrient absorption, metabolic product discharge, multi-drug resistance Important factor.

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