Imperial College London
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DrBingLiu

Faculty of Natural Sciences, Department of Life Sciences

Visiting Researcher
 
 
 
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Contact

 

+44 (0)20 7594 5464b.liu05

 
 
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Location

 

Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Liu:2023:10.1016/j.str.2023.08.005,
author = {Liu, Y and Xu, C and Zhou, H and Wang, W and Liu, B and Li, Y and Hu, X and Yu, F and He, J},
doi = {10.1016/j.str.2023.08.005},
journal = {Structure},
pages = {1463--1472.e2},
title = {The crystal structures of Sau3AI with and without bound DNA suggest a self-activation-based DNA cleavage mechanism.},
url = {http://dx.doi.org/10.1016/j.str.2023.08.005},
volume = {31},
year = {2023}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The type II restriction endonuclease Sau3AI cleaves the sequence 5'-GATC-3' in double-strand DNA producing two sticky ends. Sau3AI cuts both DNA strands regardless of methylation status. Here, we report the crystal structures of the active site mutant Sau3AI-E64A and the C-terminal domain Sau3AI-C with a bound GATC substrate. Interestingly, the catalytic site of the N-terminal domain (Sau3AI-N) is spatially blocked by the C-terminal domain, suggesting a potential self-inhibition of the enzyme. Interruption of Sau3AI-C binding to substrate DNA disrupts Sau3AI function, suggesting a functional linkage between the N- and C-terminal domains. We propose that Sau3AI-C behaves as an allosteric effector binding one GATC substrate, which triggers a conformational change to open the N-terminal catalytic site, resulting in the subsequent GATC recognition by Sau3AI-N and cleavage of the second GATC site. Our data indicate that Sau3AI and UbaLAI might represent a new subclass of type IIE restriction enzymes.
AU  - Liu,Y
AU  - Xu,C
AU  - Zhou,H
AU  - Wang,W
AU  - Liu,B
AU  - Li,Y
AU  - Hu,X
AU  - Yu,F
AU  - He,J
DO  - 10.1016/j.str.2023.08.005
EP  - 1472
PY  - 2023///
SP  - 1463
TI  - The crystal structures of Sau3AI with and without bound DNA suggest a self-activation-based DNA cleavage mechanism.
T2  - Structure
UR  - http://dx.doi.org/10.1016/j.str.2023.08.005
UR  - https://www.ncbi.nlm.nih.gov/pubmed/37652002
VL  - 31
ER  -
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