The TL29 protein is lumen located, associated with PSII and not an ascorbate peroxidase
- PMID: 19828564
- DOI: 10.1093/pcp/pcp134
The TL29 protein is lumen located, associated with PSII and not an ascorbate peroxidase
Abstract
The TL29 protein is one of the more abundant proteins in the thylakoid lumen of plant chloroplasts. Based on its sequence homology to ascorbate peroxidases, but without any supporting biochemical evidence, TL29 was suggested to be involved in the plant defense system against reactive oxygen species and consequently renamed to APX4. Our in vivo and in vitro analyses failed to show any peroxidase activity associated with TL29; it bound neither heme nor ascorbate. Recombinant overexpressed TL29 had no ascorbate-dependent peroxidase activity, and various mutational analyses aiming to convert TL29 into an ascorbate peroxidase failed. Furthermore, in the thylakoid lumen no such activity could be associated with TL29 and, additionally, TL29 knock-out mutants did not show any decreased peroxidase activity or increased content of radical oxygen species when grown under light stress. Instead we could show that TL29 is a lumen-located component associated with PSII.
Similar articles
-
Crystal structure of the TL29 protein from Arabidopsis thaliana: an APX homolog without peroxidase activity.J Struct Biol. 2011 Oct;176(1):24-31. doi: 10.1016/j.jsb.2011.07.004. Epub 2011 Jul 21. J Struct Biol. 2011. PMID: 21798352
-
Peptidyl-prolyl isomerase activity in chloroplast thylakoid lumen is a dispensable function of immunophilins in Arabidopsis thaliana.Plant Cell Physiol. 2009 Oct;50(10):1801-14. doi: 10.1093/pcp/pcp122. Epub 2009 Aug 28. Plant Cell Physiol. 2009. PMID: 19717822
-
A complex containing PGRL1 and PGR5 is involved in the switch between linear and cyclic electron flow in Arabidopsis.Cell. 2008 Jan 25;132(2):273-85. doi: 10.1016/j.cell.2007.12.028. Cell. 2008. PMID: 18243102
-
Inactivation and deficiency of core proteins of photosystems I and II caused by genetical phylloquinone and plastoquinone deficiency but retained lamellar structure in a T-DNA mutant of Arabidopsis.Plant J. 2005 Feb;41(4):627-37. doi: 10.1111/j.1365-313X.2004.02326.x. Plant J. 2005. PMID: 15686525
-
Three PsbQ-like proteins are required for the function of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis.Plant Cell Physiol. 2010 Jun;51(6):866-76. doi: 10.1093/pcp/pcq060. Epub 2010 Apr 29. Plant Cell Physiol. 2010. PMID: 20430763
Cited by
-
Cold priming on pathogen susceptibility in the Arabidopsis eds1 mutant background requires a functional stromal Ascorbate Peroxidase.Plant Signal Behav. 2024 Dec 31;19(1):2300239. doi: 10.1080/15592324.2023.2300239. Epub 2024 Jan 3. Plant Signal Behav. 2024. PMID: 38170666 Free PMC article.
-
Ascorbate Peroxidase 2 (APX2) of Chlamydomonas Binds Copper and Modulates the Copper Insertion into Plastocyanin.Antioxidants (Basel). 2023 Oct 31;12(11):1946. doi: 10.3390/antiox12111946. Antioxidants (Basel). 2023. PMID: 38001799 Free PMC article.
-
Novel insight into functions of ascorbate peroxidase in higher plants: More than a simple antioxidant enzyme.Redox Biol. 2023 Aug;64:102789. doi: 10.1016/j.redox.2023.102789. Epub 2023 Jun 16. Redox Biol. 2023. PMID: 37352686 Free PMC article. Review.
-
Comprehensive Analysis of BrHMPs Reveals Potential Roles in Abiotic Stress Tolerance and Pollen-Stigma Interaction in Brassica rapa.Cells. 2023 Apr 6;12(7):1096. doi: 10.3390/cells12071096. Cells. 2023. PMID: 37048168 Free PMC article.
-
Proteome-wide analysis of hydrogen peroxide-induced protein carbonylation in Arabidopsis thaliana.Front Plant Sci. 2022 Dec 5;13:1049681. doi: 10.3389/fpls.2022.1049681. eCollection 2022. Front Plant Sci. 2022. PMID: 36544875 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
