Back to Search Start Over

Plant catalases as NO and H2S targets

Authors :
José M. Palma
Rosa M. Mateos
Javier López-Jaramillo
Marta Rodríguez-Ruiz
Salvador González-Gordo
Alfonso M. Lechuga-Sancho
Francisco J. Corpas
Source :
Redox Biology, Vol 34, Iss , Pp 101525- (2020)
Publication Year :
2020
Publisher :
Elsevier, 2020.

Abstract

Catalase is a powerful antioxidant metalloenzyme located in peroxisomes which also plays a central role in signaling processes under physiological and adverse situations. Whereas animals contain a single catalase gene, in plants this enzyme is encoded by a multigene family providing multiple isoenzymes whose number varies depending on the species, and their expression is regulated according to their tissue/organ distribution and the environmental conditions. This enzyme can be modulated by reactive oxygen and nitrogen species (ROS/RNS) as well as by hydrogen sulfide (H2S). Catalase is the major protein undergoing Tyr-nitration [post-translational modification (PTM) promoted by RNS] during fruit ripening, but the enzyme from diverse sources is also susceptible to undergo other activity-modifying PTMs. Data on S-nitrosation and persulfidation of catalase from different plant origins are given and compared here with results from obese children where S-nitrosation of catalase occurs. The cysteine residues prone to be S-nitrosated in catalase from plants and from bovine liver have been identified. These evidences assign to peroxisomes a crucial statement in the signaling crossroads among relevant molecules (NO and H2S), since catalase is allocated in these organelles. This review depicts a scenario where the regulation of catalase through PTMs, especially S-nitrosation and persulfidation, is highlighted.

Details

Language :
English
ISSN :
22132317
Volume :
34
Issue :
101525-
Database :
Directory of Open Access Journals
Journal :
Redox Biology
Publication Type :
Academic Journal
Accession number :
edsdoj.5f82f1484abc4c8ba716b656f1cf5806
Document Type :
article
Full Text :
https://doi.org/10.1016/j.redox.2020.101525