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Phosphoproteome modulation by nucleoside diphosphate kinase affects photosynthesis & stress tolerance of Nostoc PCC 7120.

Authors :
Kirti A
Rajaram H
Source :
Biochimica et biophysica acta. Proteins and proteomics [Biochim Biophys Acta Proteins Proteom] 2025 Jan 01; Vol. 1873 (1), pp. 141054. Date of Electronic Publication: 2024 Oct 09.
Publication Year :
2025

Abstract

Nucleoside diphosphate kinase (Ndk/NDK/NDPK) is known to possess pleiotropic functions, one of which is that as a protein kinase, and has been shown to be involved in stress tolerance in plants. To assess its role in the cyanobacterium Nostoc PCC 7120, which is hitherto unreported, recombinant strain overexpressing Ndk, Anndk <superscript>+</superscript> was generated. Phosphoproteomic analysis of Anndk <superscript>+</superscript> and its comparison with that of the vector control, AnpAM, revealed differential phosphorylation at S/T/Y sites of proteins belonging to varied functional groups, with over 17 % phosphoproteins involved in photosynthesis. A total of 177 phosphopeptides and 117 phosphoproteins were identified, including newly identified phosphopeptides in any cyanobacteria. Compared to AnpAM, the Anndk <superscript>+</superscript> cells exhibited (i) lower photosynthetic efficiency and electron transport rate at low PAR (photosynthetically active radiation), (ii) no change in photochemical quenching across PAR, (iii) but distinct non-photochemical quenching [zero Y(NPQ) and high Y(NO) in Anndk <superscript>+</superscript> and high Y(NPQ) and low (NO) in AnpAM], and (iv) increased tolerance to γ-radiation, oxidative, salt and DCMU stresses. The observed modulation of phosphoproteome linked to physiological changes upon overexpression of Ndk in Nostoc could be a combination of direct protein kinase activity of Ndk and/or indirectly through other protein kinases and phosphatases whose phosphorylation status is mediated by Ndk. This is the first report on a direct correlation between Ndk levels, phosphorylation status of proteins and stress tolerance in any cyanobacteria.<br />Competing Interests: Declaration of competing interest Authors report no conflict of interest.<br /> (Copyright © 2024 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1878-1454
Volume :
1873
Issue :
1
Database :
MEDLINE
Journal :
Biochimica et biophysica acta. Proteins and proteomics
Publication Type :
Academic Journal
Accession number :
39389524
Full Text :
https://doi.org/10.1016/j.bbapap.2024.141054