Research output: Contribution to journal › Article › peer-review
N-Acetyl-L-glutamate Kinase of Chlamydomonas reinhardtii: In Vivo Regulation by PII Protein and Beyond. / Власова, Виталина Анатольевна; Лапина, Татьяна Викторовна; Статинов, Владислав Романович; Ермилова, Елена Викторовна.
In: International Journal of Molecular Sciences, Vol. 24, No. 16, 12873, 17.08.2023.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - N-Acetyl-L-glutamate Kinase of Chlamydomonas reinhardtii: In Vivo Regulation by PII Protein and Beyond
AU - Власова, Виталина Анатольевна
AU - Лапина, Татьяна Викторовна
AU - Статинов, Владислав Романович
AU - Ермилова, Елена Викторовна
PY - 2023/8/17
Y1 - 2023/8/17
N2 - N-Acetyl-L-glutamate kinase (NAGK) catalyzes the rate-limiting step in the ornithine/arginine biosynthesis pathway in eukaryotic and bacterial oxygenic phototrophs. NAGK is the most highly conserved target of the PII signal transduction protein in Cyanobacteria and Archaeplastida (red algae and Chlorophyta). However, there is still much to be learned about how NAGK is regulated in vivo. The use of unicellular green alga Chlamydomonas reinhardtii as a model system has already been instrumental in identifying several key regulation mechanisms that control nitrogen (N) metabolism. With a combination of molecular-genetic and biochemical approaches, we show the existence of the complex CrNAGK control at the transcriptional level, which is dependent on N source and N availability. In growing cells, CrNAGK requires CrPII to properly sense the feedback inhibitor arginine. Moreover, we provide primary evidence that CrPII is only partly responsible for regulating CrNAGK activity to adapt to changing nutritional conditions. Collectively, our results suggest that in vivo CrNAGK is tuned at the transcriptional and post-translational levels, and CrPII and additional as yet unknown factor(s) are integral parts of this regulation.
AB - N-Acetyl-L-glutamate kinase (NAGK) catalyzes the rate-limiting step in the ornithine/arginine biosynthesis pathway in eukaryotic and bacterial oxygenic phototrophs. NAGK is the most highly conserved target of the PII signal transduction protein in Cyanobacteria and Archaeplastida (red algae and Chlorophyta). However, there is still much to be learned about how NAGK is regulated in vivo. The use of unicellular green alga Chlamydomonas reinhardtii as a model system has already been instrumental in identifying several key regulation mechanisms that control nitrogen (N) metabolism. With a combination of molecular-genetic and biochemical approaches, we show the existence of the complex CrNAGK control at the transcriptional level, which is dependent on N source and N availability. In growing cells, CrNAGK requires CrPII to properly sense the feedback inhibitor arginine. Moreover, we provide primary evidence that CrPII is only partly responsible for regulating CrNAGK activity to adapt to changing nutritional conditions. Collectively, our results suggest that in vivo CrNAGK is tuned at the transcriptional and post-translational levels, and CrPII and additional as yet unknown factor(s) are integral parts of this regulation.
KW - Arginine
KW - Biotin
KW - Chlamydomonas reinhardtii/genetics
KW - Eukaryota
KW - green algae
KW - PII- signal transduction protein
KW - arginine biosynthesis
KW - N-Acetyl-L-glutamate kinase
UR - https://www.mendeley.com/catalogue/1ef87538-c32d-3257-b2b6-832d08f6b7fa/
U2 - 10.3390/ijms241612873
DO - 10.3390/ijms241612873
M3 - Article
C2 - 37629055
VL - 24
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
SN - 1422-0067
IS - 16
M1 - 12873
ER -
ID: 108273196