PEPR1 and PEPR2
editIntroduction
editPEPR 1 and PEPR2 are homolog kinases that act as enzymes on other proteins. They attach a phosphate group to specific proteins, called phosphorylation. These reactions can cause the function of the phosphorylated proteins to change. Both PEPR 1 and PEPR 2 can be classified as receptor kinases, which serve an important role in immunity in plants. Receptor kinases have the ability to change the conformation of receptors by adding the phosphate group. These specific receptor kinases serve as a pattern recognition receptor, or PRR, that can quickly and efficiently recognize many different molecular patterns or signatures that are unique to each pathogen. They can also detect different danger signals released from the host and respond accordingly. More specifically, the proteins contain leucine-rich repeat segments that interact outside of the cell. This leucine-rich repeat is a structural motif present in some proteins that has specific functions due to its folded structure. This fold can contain many repeating amino acids, but the most common is the hydrophobic leucine, hence the name. PEPR1 and PEPR2 are present in plants and are involved in several immune system processes[1]. Their ability to change the conformation of receptors can have an effect on signaling processes within plants, allowing the plant to have a system of immunity in place in case of an infection or pathogen.
PEPR 1 and PEPR2 have been studied by multiple researchers for their properties and functions in immune system processes. Many of these studies involve isolating and crystallizing the proteins[1] and have been performed in the natural setting, in vivo, as well as in an artificial lab environment, in vitro. The proteins function as inhibitors that potentially help plants have immunity to different substances by working with other compounds in the plant. Pep1, a receptor in the plant, can be controlled by PEPR1 and PEPR2, along with other proteins and enzymes such as “botrytis-induced kinase 1 (BIK1) and PBS1-like 1 (PBL1)” [2]. More specifically, when exposed to the Pep1 receptor, the proteins act as kinases when interacting with BIK1[2].
References
edit- ^ a b Tang, Jiao; Han, Zhifu; Sun, Yadonf; Zhang, Heqiao; Gong, Xinqi; Chai, Jijie (2015). "Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1". Cell Research. 25 (1): 110–120.
{{cite journal}}:|access-date=requires|url=(help) - ^ a b Liu, Zixu; Wu, Ying; Yang, Fan; Zhang, Yiyue; Chen, She; Xie, Qi; Tian, Xingjun; Zhou, Jian-Min (9 April 2013). [www.pnas.org/cgi/doi/10.1073/pnas.1215543110 "BIK1 interacts with PEPRs to mediate ethylene-induced immunity"]. Proceedings of the National Academy of Sciences. 110 (15): 6205–6210. doi:10.1073/pnas.1215543110. ISSN 0027-8424.
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