Calcium signaling in plant-microbe interaction: Difference between revisions

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The first step of a Ca<sup>2+</sup> signaling event is the detection of microbes performed by pattern-recognition receptors (PRRs), a type of receptor protein located on the plasma membrane of a plant cell. PRRs are capable of recognizing microbe-associated molecular patterns (MAMPs), molecules specific to certain classes of microbes that are present in extracellular space.<ref>[https://apsjournals.apsnet.org/doi/full/10.1094/MPMI-08-20-0239-IA Lu, You, and Tsuda, Kenichi. “Intimate Association of PRR- and NLR-Mediated Signaling in Plant Immunity” 2020. Molecular Plant-Microbe Interactions 34(1): 3-14.]</ref><br>
The first step of a Ca<sup>2+</sup> signaling event is the detection of microbes performed by pattern-recognition receptors (PRRs), a type of receptor protein located on the plasma membrane of a plant cell. PRRs are capable of recognizing microbe-associated molecular patterns (MAMPs), molecules specific to certain classes of microbes that are present in extracellular space.<ref>[https://apsjournals.apsnet.org/doi/full/10.1094/MPMI-08-20-0239-IA Lu, You, and Tsuda, Kenichi. “Intimate Association of PRR- and NLR-Mediated Signaling in Plant Immunity” 2020. Molecular Plant-Microbe Interactions 34(1): 3-14.]</ref><br>
===Bacteria===
===Bacteria===
All PRRs that can recognize MAMPs of bacteria studied so far are either receptor-like kinase or receptor-like protein. All of them are transmembrane receptors.<ref>[https://www.sciencedirect.com/science/article/pii/S136952741000192X Segonzac, Cécile and Zipfel, Cyril. “Activation of plant pattern-recognition receptors by bacteria” 2011. Current Opinion in Microbiology 14(1): 54-61.]</ref> One example of these PRRs is flagellin-sensitive 2 (FLS2), which recognizes the flagellin protein in bacteria flagellum.<ref>[https://www.nature.com/articles/nature05999 Chinchilla, D. et al. “A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence” 2007. Nature 448: 497-500]</ref> MAMPs of symbiotic bacteria can also be recognized by PPRs. A lysin-motif (LysM) receptor-like kinase, nodulation (nod) factor perception (NFP), can recognize lipochitooligosaccharide in the nod factor released by symbiotic bacteria such as rhizobia.<ref>[https://www.sciencedirect.com/science/article/pii/S1360138513001088 Gough, Clare and Jacquet Christophe. “Nod factor perception protein carries weight in biotic interactions” 2013. Trends in Plant Science 18(10): 566-574]</ref><br>
All PRRs that can recognize MAMPs of bacteria studied so far are either receptor-like kinase or receptor-like protein. All of them are transmembrane receptors.<ref>[https://www.sciencedirect.com/science/article/pii/S136952741000192X Segonzac, Cécile and Zipfel, Cyril. “Activation of plant pattern-recognition receptors by bacteria” 2011. Current Opinion in Microbiology 14(1): 54-61.]</ref> One example of these PRRs is flagellin-sensitive 2 (FLS2), which recognizes the flagellin protein in bacteria flagellum.<ref>[https://www.nature.com/articles/nature05999 Chinchilla, D. et al. “A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence” 2007. Nature 448: 497-500.]</ref> MAMPs of symbiotic bacteria can also be recognized by PPRs. A lysin-motif (LysM) receptor-like kinase, nodulation (nod) factor perception (NFP), can recognize lipochitooligosaccharide in the nod factor released by symbiotic bacteria such as rhizobia.<ref>[https://www.sciencedirect.com/science/article/pii/S1360138513001088 Gough, Clare and Jacquet Christophe. “Nod factor perception protein carries weight in biotic interactions” 2013. Trends in Plant Science 18(10): 566-574.]</ref><br>


==Formation of Calcium Signature==
==Formation of Calcium Signature==

Revision as of 19:34, 5 December 2021

Introduction

Calcium ion (Ca2+) is an important second messenger involved in many signaling pathways in plants.[1] The concentration of free Ca2+ in the cytosol in a plant cell ([Ca2+]cyt) connects the extracellular stimuli, including the signal of microbes, to intracellular responses. Since Ca2+ is neither synthesized nor degraded by plants, [Ca2+]cytis completely dependent on the entry of external source or release of Ca2+ from its intracellular stores.[2][3] However, because Ca2+ can react with phosphate, the energy source of life, its presence in the cytoplasm will prevent energy metabolism and other cellular activities from taking place.[4] Thus, its concentration is regulated tightly by various proteins. In plant-microbe interaction, different microbes trigger different receptor proteins, causing distinctive Ca2+ elevation patterns, referred to as Ca2+ signature. Ca2+ signature can be different from each other in various aspects: amplitude, duration, frequency, spatial distribution, and times of cycle in [Ca2+]cytchanges. The Ca2+ signature produced by microbe signal can be decoded by downstream effectors, changing the expression of defense or symbiosis-related genes, resulting in different responses by plants.[5]

Detection of Microbes

The first step of a Ca2+ signaling event is the detection of microbes performed by pattern-recognition receptors (PRRs), a type of receptor protein located on the plasma membrane of a plant cell. PRRs are capable of recognizing microbe-associated molecular patterns (MAMPs), molecules specific to certain classes of microbes that are present in extracellular space.[6]

Bacteria

All PRRs that can recognize MAMPs of bacteria studied so far are either receptor-like kinase or receptor-like protein. All of them are transmembrane receptors.[7] One example of these PRRs is flagellin-sensitive 2 (FLS2), which recognizes the flagellin protein in bacteria flagellum.[8] MAMPs of symbiotic bacteria can also be recognized by PPRs. A lysin-motif (LysM) receptor-like kinase, nodulation (nod) factor perception (NFP), can recognize lipochitooligosaccharide in the nod factor released by symbiotic bacteria such as rhizobia.[9]

Formation of Calcium Signature


Decoding of Calcium Signature


Conclusion


References


Edited by Yueqi Song, student of Joan Slonczewski for BIOL 116 Information in Living Systems, 2021, Kenyon College.