Volume 5 Issue 4
Apr.  2014
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Dong Deng, Chuangye Yan, Jianping Wu, Xiaojing Pan, Nieng Yan. Revisiting the TALE repeat[J]. Protein&Cell, 2014, 5(4): 297-306. doi: 10.1007/s13238-014-0035-2
Citation: Dong Deng, Chuangye Yan, Jianping Wu, Xiaojing Pan, Nieng Yan. Revisiting the TALE repeat[J]. Protein&Cell, 2014, 5(4): 297-306. doi: 10.1007/s13238-014-0035-2

Revisiting the TALE repeat

doi: 10.1007/s13238-014-0035-2
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We thank J. He and S. Huang for crystal screening at Shanghai Synchrotron Radiation Facility (SSRF). This work was supported by funds from the National Basic Research Program (973 Program) (No. 2011CB910501), the National Natural Science Foundation of China (Grant Nos. 31125009 and 91017011), and funds from Tsinghua University. The research of Nieng Yan was supported in part by an International Early Career Scientist grant from the Howard Hughes Medical Institute. Coordinates and structure factors for the TAL effector structures have been deposited with the Protein Data Bank under accession codes 4OSH, 4OSI, 4OSJ, 4OSK, 4OSL, 4OSM, 4OSQ, 4OSR, 4OSS, 4OST, 4OSV, 4OSW, 4OSZ, 4OT0, 4OT3 and 4OTO.

  • Received Date: 2013-12-06
  • Rev Recd Date: 2014-02-12
  • Transcription activator-like (TAL) effectors specifically bind to double stranded (ds) DNA through a central domain of tandem repeats. Each TAL effector (TALE) repeat comprises 33-35 amino acids and recognizes one specific DNA base through a highly variable residue at a fixed position in the repeat. Structural studies have revealed the molecular basis of DNA recognition by TALE repeats. Examination of the overall structure reveals that the basic building block of TALE protein, namely a helical hairpin, is one-helix shifted from the previously defined TALE motif. Here we wish to suggest a structure-based re-demarcation of the TALE repeat which starts with the residues that bind to the DNA backbone phosphate and concludes with the base-recognition hyper-variable residue. This new numbering system is consistent with the α-solenoid superfamily to which TALE belongs, and reflects the structural integrity of TAL effectors. In addition, it confers integral number of TALE repeats that matches the number of bound DNA bases. We then present fifteen crystal structures of engineered dHax3 variants in complex with target DNA molecules, which elucidate the structural basis for the recognition of bases adenine (A) and guanine (G) by reported or uncharacterized TALE codes. Finally, we analyzed the sequence-structure correlation of the amino acid residues within a TALE repeat. The structural analyses reported here may advance the mechanistic understanding of TALE proteins and facilitate the design of TALEN with improved affinity and specificity.
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