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Potential Role of the Last Half Repeat in TAL Effectors Revealed by a Molecular Simulation Study.

Abstract：

:TAL effectors (TALEs) contain a modular DNA-binding domain that is composed of tandem repeats. In all naturally occurring TALEs, the end of tandem repeats is invariantly a truncated half repeat. To investigate the potential role of the last half repeat in TALEs, we performed comparative molecular dynamics simulations for the crystal structure of DNA-bound TALE AvrBs3 lacking the last half repeat and its modeled structure having the last half repeat. The structural stability analysis indicates that the modeled system is more stable than the nonmodeled system. Based on the principle component analysis, it is found that the AvrBs3 increases its structural compactness in the presence of the last half repeat. The comparison of DNA groove parameters of the two systems implies that the last half repeat also causes the change of DNA major groove binding efficiency. The following calculation of hydrogen bond reveals that, by stabilizing the phosphate binding with DNA at the C-terminus, the last half repeat helps to adopt a compact conformation at the protein-DNA interface. It further mediates more contacts between TAL repeats and DNA nucleotide bases. Finally, we suggest that the last half repeat is required for the high-efficient recognition of DNA by TALE.

journal_name

Biomed Res Int

journal_title

BioMed research international

authors

Wan H,Chang S,Hu JP,Tian XH,Wang MH

doi

10.1155/2016/8036450

subject

Has Abstract

pub_date

2016-01-01 00:00:00

pages

8036450

eissn

2314-6133

issn

2314-6141

journal_volume

2016

pub_type

杂志文章

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