Role of H 2 S in plants: a current update
Hydrogen Sulfide in Plant Biology, Page: 133-147
2021
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Book Chapter Description
The biological diversity in plants demands dual roles of some compounds. As a result, compounds like hydrogen sulfide (H 2 S), which were earlier considered only as harmful to the plants, are recently being recognized as useful signaling molecules because of their diverse roles in modulating the growth and physiological processes of plants. After nitric oxide (NO) and carbon monoxide (CO), H 2 S is considered to be the third endogenous gasotransmitter in plants. Its ubiquity and useful properties have recently brought it to the attention of plant physiologists and biochemists. It has three main roles in plants: as a substrate, as a toxin, and as a signal. H 2 S was mainly generated in vivo as an endogenous neural active substance but now it is emerging as a signaling molecule. L-cysteine desulfhydrase (LCD) and D-cysteine desulfhydrase (DCD) were primarily known to generate H 2 S from the degradation of cysteine. H 2 S regulates various biochemical and physiological functions in plants such as germination, various growth and developmental phases of plants, regulation of defense responses, senescence, and maturation. H 2 S also has potential to induce the accumulation of osmoprotectants to protect plants from osmotic stress, improve enzymatic and nonenzymatic cellular antioxidants, modulate the cell cycle, apoptosis, and reduce the oxidative stress caused by reactive oxygen species. H 2 S enhances plant response to various stressful environmental conditions by mitigating injuries and toxicities caused by them. H 2 S also interacts with the other signaling molecules like carbon monoxide (CO), hydrogen peroxide (H 2 O 2 ), Ca 2+, nitric oxide (NO), and other molecules in signaling pathways. The main signaling pathway through which H 2 S regulates protein functions is persulfidation, cysteine-dependent posttranslational modification (PTM). This PTM may cause functional alterations in structures and activities of protein and subcellular positions of the target proteins.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/B978032385862500004X; http://dx.doi.org/10.1016/b978-0-323-85862-5.00004-x; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85128037132&origin=inward; https://linkinghub.elsevier.com/retrieve/pii/B978032385862500004X; https://dx.doi.org/10.1016/b978-0-323-85862-5.00004-x
Elsevier BV
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