The NAD Kinase Slr0400 Functions as a Growth Repressor in Synechocystis sp. PCC 6803.


Journal

Plant & cell physiology
ISSN: 1471-9053
Titre abrégé: Plant Cell Physiol
Pays: Japan
ID NLM: 9430925

Informations de publication

Date de publication:
24 Sep 2021
Historique:
received: 19 08 2020
accepted: 04 02 2021
pubmed: 10 2 2021
medline: 21 10 2021
entrez: 9 2 2021
Statut: ppublish

Résumé

NADP+, the phosphorylated form of nicotinamide adenine dinucleotide (NAD), plays an essential role in many cellular processes. NAD kinase (NADK), which is conserved in all living organisms, catalyzes the phosphorylation of NAD+ to NADP+. However, the physiological role of phosphorylation of NAD+ to NADP+ in the cyanobacterium Synechocystis remains unclear. In this study, we report that slr0400, an NADK-encoding gene in Synechocystis, functions as a growth repressor under light-activated heterotrophic growth conditions and light and dark cycle conditions in the presence of glucose. We show, via characterization of NAD(P)(H) content and enzyme activity, that NAD+ accumulation in slr0400-deficient mutant results in the unsuppressed activity of glycolysis and tricarboxylic acid (TCA) cycle enzymes. In determining whether Slr0400 functions as a typical NADK, we found that constitutive expression of slr0400 in an Arabidopsis nadk2-mutant background complements the pale-green phenotype. Moreover, to determine the physiological background behind the growth advantage of mutants lacking slr04000, we investigated the photobleaching phenotype of slr0400-deficient mutant under high-light conditions. Photosynthetic analysis found in the slr0400-deficient mutant resulted from malfunctions in the Photosystem II (PSII) photosynthetic machinery. Overall, our results suggest that NADP(H)/NAD(H) maintenance by slr0400 plays a significant role in modulating glycolysis and the TCA cycle to repress the growth rate and maintain the photosynthetic capacity.

Identifiants

pubmed: 33560438
pii: 6131679
doi: 10.1093/pcp/pcab023
doi:

Substances chimiques

Arabidopsis Proteins 0
Bacterial Proteins 0
Adenosine Diphosphate 61D2G4IYVH
Adenosine Triphosphate 8L70Q75FXE
Phosphotransferases (Alcohol Group Acceptor) EC 2.7.1.-
NAD kinase EC 2.7.1.23
NADK2 protein, Arabidopsis EC 2.7.1.23

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

668-677

Subventions

Organisme : KAKENHI
ID : 17H05714

Informations de copyright

© The Author(s) 2021. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oup.com.

Auteurs

Yuuma Ishikawa (Y)

Institute for Molecular Physiology and Cluster of Excellence on Plant Sciences (CEPLAS), Heinrich-Heine-University Düsseldorf, Düsseldorf 40225, Germany.
Institute of Transformative Bio-Molecules (WPI-ITbM), Nagoya University, Chikusa, Nagoya, 464-8601 Japan.
Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Cedric Cassan (C)

UMR1332 Biologie du Fruit et Pathologie and Plateforme Métabolome, Centre de Génomique Fonctionnelle Bordeaux, INRA-Bordeaux and Bordeaux University, Villenave d'Ornon, France.

Aikeranmu Kadeer (A)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Koki Yuasa (K)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Nozomu Sato (N)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Kintake Sonoike (K)

Faculty of Education and Integrated Arts and Sciences, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo, 162-8480 Japan.

Yasuko Kaneko (Y)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Atsuko Miyagi (A)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Hiroko Takahashi (H)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Toshiki Ishikawa (T)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Masatoshi Yamaguchi (M)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Yoshitaka Nishiyama (Y)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Yukako Hihara (Y)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

Yves Gibon (Y)

UMR1332 Biologie du Fruit et Pathologie and Plateforme Métabolome, Centre de Génomique Fonctionnelle Bordeaux, INRA-Bordeaux and Bordeaux University, Villenave d'Ornon, France.

Maki Kawai-Yamada (M)

Graduate School of Science and Engineering, Saitama University, 225 Shimo-Okubo, Sakura-ku, Saitama City, Saitama, 338-8570 Japan.

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