Abstract

Xanthomonas oryzae pv. oryzae (Xoo) is a plant pathogen that causes bacterial blight of rice, with outbreaks occurring in most rice-growing countries. Thus far, there is no effective pesticide against bacterial blight. Chaperones in bacterial pathogens are important for the stabilization and delivery of effectors into host cells to cause disease. In bacteria, GroEL/GroES complex mediates protein folding and protects proteins against misfolding and aggregation caused by environmental stress. We determined the crystal structure of GroEL from Xanthomonas oryzae pv. oryzae (XoGroEL) at 3.2 Å resolution, which showed the open form of two conserved homoheptameric rings stacked back-to-back. In the open form structure, the apical domain of XoGroEL had a higher B factor than the intermediate and equatorial domains, indicating that the apical domain had a flexible conformation before the binding of substrate unfolded protein and ATP. The XoGroEL structure will be helpful in understanding the function and catalytic mechanism of bacterial chaperonin GroELs.

Highlights

  • Rice is the most cultivated food crop, feeding more than half of the world population [1]

  • Type III secretion system (T3SS) encoded by hrp genes is essential for the pathogenicity of Xanthomonas oryzae pv. oryzae (Xoo), via which virulent T3 effector proteins are delivered to rice to modulate the host system for disease progress [4]

  • The T3SS consists of a narrow, needle-like structure such as pili, within which T3 effectors should be translocated to host rice [5]

Read more

Summary

Introduction

Rice is the most cultivated food crop, feeding more than half of the world population [1]. Oryzae (Xoo) causes bacterial blight, which is one of the most problematic diseases in rice and can cause crop losses of up to 50% [3]. Type III secretion system (T3SS) encoded by hrp genes is essential for the pathogenicity of Xoo, via which virulent T3 effector proteins are delivered to rice to modulate the host system for disease progress [4]. The T3SS consists of a narrow, needle-like structure such as pili, within which T3 effectors should be translocated to host rice [5]. Chaperones in Xoo play a role in stabilizing effector proteins before the delivery to host [6,7]

Methods
Results
Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call