Abstract:

RPM1-interacting protein 4 (RIN4) is a multidomain and versatile immune system regulatory protein (R-protein family) that is involved in plant defence mechanisms against bacterial type III effector proteins (T3Es) and pathogen-associated molecular patterns (PAMPS). PAMPs and T3Es are recognized by innate plant immune systems such as PAMP-triggered immunity (PTI) and effector-triggered immunity (ETI). RIN4 is a linker protein that is a bridge between PTI and ETI. Different domains of RIN4 play different roles in the mechanism of phytoimmunity. Separable fragments of RIN4 include two domains; ACP2 (11-152) and ACP3 (153-211). ACP2 is the N-terminal domain of RIN4 and ACP3 lies in the C-terminal part. RIN4 negatively regulates the RPS2 (Resistant to P. syringae2) protein thereby keeping the immune response active. The aim of this project is to determine the structural basis of immune regulation involving different domains of RIN4. In this regard, we aim to produce the ACP2 and ACP3 domains of RIN4, study their interactions with RPS2 or other substrates and solve the structure of the corresponding RIN4 domain using NMR techniques.

Evaluation Committee:

• Dr. Syed Shahzad ul Hussan
• Dr. Khurram Bashir