电邮这篇文章 Effect of the PotN Protein on Activities of the GlnR and PotA Proteins in the Cells of Lentilactobacillus hilgardii
- 作者: Iskhakova Z.I.1, Zhuravleva D.E.1, Kayumov A.R.1
-
隶属关系:
- Kazan (Volga Region) Federal University
- 期: 卷 93, 编号 2 (2024)
- 页面: 193-197
- 栏目: SHORT COMMUNICATIONS
- URL: https://ogarev-online.ru/0026-3656/article/view/262523
- DOI: https://doi.org/10.31857/S0026365624020173
- ID: 262523
如何引用文章
开放存取
##reader.subscriptionAccessGranted##
详细
Bacterial PII-like proteins are global regulators of nitrogen and energy metabolism, which respond to nutrient availability by binding their partner proteins, thus modulating their activity. The PotN protein from Lentilactobacillus hilgardii, a member of the new family of PII-like proteins, is capable of competitive binding of ATP and ADP, thus regulating metabolism in response to the cell energy status. Thus, under ADP excess, PotN binds this nucleotide and interacts mostly with the PotA subunit of the polyamine АВС transporter, suppressing its ATPase activity. PotN also dissociates from the transcription factor GlnR, restoring its ability to bind DNA and modulate expression of the genes of the GlnR regulon. On the contrary, in the ATP state PotN dissociates from PotA and binds to the GlnR factor.
全文:
作者简介
Z. Iskhakova
Kazan (Volga Region) Federal University
编辑信件的主要联系方式.
Email: zalinunya@mail.ru
俄罗斯联邦, Kazan, 420008
D. Zhuravleva
Kazan (Volga Region) Federal University
Email: zalinunya@mail.ru
俄罗斯联邦, Kazan, 420008
A. Kayumov
Kazan (Volga Region) Federal University
Email: zalinunya@mail.ru
俄罗斯联邦, Kazan, 420008
参考
- Журавлева Д.Э. Регулон фактора транскрипции GlnR в клетках Lentilactobacillus hilgardii и механизм регуляции его ДНК-связывающей активности. Автореферат дис. … канд. биол. наук, 28.12.2021. Казань: Казанский федеральный университет, 2021. 24 с.
- Каюмов А.Р. Молекулярные механизмы регуляции азотного обмена грамположительных бактерий. Автореферат дис. … докт. биол. наук, 24.01.2019. Казань: Казанский федеральный университет, 2018. 40 с.
- Forchammer K., Selim K.A., Huergo L.F. New views on PII signaling: from nitrogen sensing to global metabolic control // Trends Microbiol. 2022. V. 30. P. 733‒735.
- Gerhardt E.C.M., Parize E., Gravina F., Pontes F.L.D., Santos A.R.S., Araújo G.A.T., Goedert A.C., Urbanski A.H., Steffens M.B.R., Chubatsu L.S., Pedrosa F.O., Souza E.M., Forchhammer K., Ganusova E., Alexandre G., de Souza G.A., Huergo L.F. The protein–protein interaction network reveals a novel role of the signal transduction protein PII in the control of c-di-GMP homeostasis in Azospirillum brasilense // mSystems. 2020. V. 5. Art. e00817–20.
- Grau F.C., Burkovski A., Muller Y.A. Crystal structures of adenylylated and unadenylylated PII protein GlnK from Corynebacterium glutamicum // Acta Crystallogr. D Struct. Biol. 2021. V. 77. P. 325‒335.
- Igarashi K., Kashiwagi K. Modulation of cellular function by polyamines // Int. J. Biochem. Cell Biol. 2010. V. 42. P. 39‒51.
- Iskhakova Z., Zhuravleva D., Laykov A., Forchhammer K., Kayumov A. The preliminary characterization of P-II like protein GlnK from Lactobacillus brevis // FEBS J. 2016. V. 283. P. 228.
- Iskhakova Z., Zhuravleva D.E., Heim C., Hartmann M.D., Laykov A.V., Forchhammer K., Kayumov A.R. PotN represents a novel energy-state sensing PII subfamily, occurring in firmicutes // FEBS J. 2022. V. 289. P. 5305‒5321.
- Lanzetta P.A., Alvarez L.J., Reinach P.S., Candia O.A. An improved assay for nanomole amounts of inorganic phosphate // Anal. Biochem. 1979. V. 100. P. 95‒97.
- Lüddecke J., Forchhammer K. From PII signaling to metabolite sensing: a novel 2-oxoglutarate sensor that details PII-NAGK complex formation // PLoS. One. 2013. V. 8. Art. e83181.
- Santos A.R.S., Gerhardt E.C.M., Parize E., Pedrosa F.O., Steffens M.B.R., Chubatsu L.S., Souza E.M., Passaglia L.M.P., Sant’Anna F.H., de Souza G.A., Huergo L.F. NAD+ biosynthesis in bacteria is controlled by global carbon/nitrogen levels via PII signaling // J. Biol. Chem. 2020. V. 295. P. 6165‒6176.
- Selim K.A., Lapina T., Forchhammer K., Ermilova E. Interaction of N-acetyl-l-glutamate kinase with the PII signal transducer in the non-photosynthetic alga Polytomella parva: co-evolution towards a hetero-oligomeric enzyme // FEBS J. 2020. V. 287. P. 465‒482.
- Xu M., Tang M., Chen J., Yang T., Zhang X., Shao M., Xu Z., Rao Z. PII signal transduction protein GlnK alleviates feedback inhibition of N-acetyl-l-glutamate kinase by l-arginine in Corynebacterium glutamicum // Appl. Environ. Microbiol. 2020. V. 86. Art. e00039-20.
- Zhuravleva D.E., Iskhakova Z.I., Ozhegov G.D., Gogoleva N.E., Khusnutdinova D.R., Shagimardanova E.I., Forchhammer K., Kayumov A.R. Complete genome sequence of Lactobacillus hilgardii LMG 7934, carrying the gene encoding for the novel PII-like protein PotN // Curr. Microbiol. 2020. V. 77. P. 3538‒3545.
补充文件
