Dissection of the Mechanisms of Growth Inhibition Resulting from Loss of the PII Protein in the Cyanobacterium Synechococcus elongatus PCC 7942.

Autor: Sakamoto T; Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601 Japan., Takatani N; Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601 Japan., Sonoike K; Faculty of Education and Integrated Arts and Sciences, Waseda University, Tokyo, 162-8480 Japan., Jimbo H; Graduate School of Science and Engineering, Saitama University, Saitama, 338-8570 Japan.; Graduate School of Arts and Sciences, University of Tokyo,Tokyo 153-8902Japan., Nishiyama Y; Graduate School of Science and Engineering, Saitama University, Saitama, 338-8570 Japan., Omata T; Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601 Japan.
Jazyk: angličtina
Zdroj: Plant & cell physiology [Plant Cell Physiol] 2021 Sep 24; Vol. 62 (4), pp. 721-731.
DOI: 10.1093/pcp/pcab030
Abstrakt: In cyanobacteria, the PII protein (the glnB gene product) regulates a number of proteins involved in nitrogen assimilation including PipX, the coactivator of the global nitrogen regulator protein NtcA. In Synechococcus elongatus PCC 7942, construction of a PII-less mutant retaining the wild-type pipX gene is difficult because of the toxicity of uncontrolled action of PipX and the other defect(s) resulting from the loss of PIIper se, but the nature of the PipX toxicity and the PipX-independent defect(s) remains unclear. Characterization of a PipX-less glnB mutant (PD4) in this study showed that the loss of PII increases the sensitivity of PSII to ammonium. Ammonium was shown to stimulate the formation of reactive oxygen species in the mutant cells. The ammonium-sensitive growth phenotype of PD4 was rescued by the addition of an antioxidant α-tocopherol, confirming that photo-oxidative damage was the major cause of the growth defect. A targeted PII mutant retaining wild-type pipX was successfully constructed from the wild-type S. elongatus strain (SPc) in the presence of α-tocopherol. The resulting mutant (PD1X) showed an unusual chlorophyll fluorescence profile, indicating extremely slow reduction and re-oxidation of QA, which was not observed in mutants defective in both glnB and pipX. These results showed that the aberrant action of uncontrolled PipX resulted in an impairment of the electron transport reactions in both the reducing and oxidizing sides of QA.
(© The Author(s) 2021. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists.)
Databáze: MEDLINE
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