{"title":"Effect of the PotN Protein on Activities of the GlnR and PotA Proteins in the Cells of Lentilactobacillus hilgardii","authors":"Z. I. Iskhakova, D. E. Zhuravleva, A. R. Kayumov","doi":"10.1134/s0026261723604177","DOIUrl":null,"url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>Bacterial PII-like proteins are global regulators of nitrogen and energy metabolism, which respond to nutrients availability by binding cognate partner proteins, thus modulating their activity. The PotN protein from <i>Lentilactobacillus hilgardii</i>, 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.</p>","PeriodicalId":18514,"journal":{"name":"Microbiology","volume":"58 1","pages":""},"PeriodicalIF":1.3000,"publicationDate":"2024-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Microbiology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1134/s0026261723604177","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Bacterial PII-like proteins are global regulators of nitrogen and energy metabolism, which respond to nutrients availability by binding cognate 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.
期刊介绍：
Microbiology is an is an international peer reviewed journal that covers a wide range of problems in the areas of fundamental and applied microbiology. The journal publishes experimental and theoretical papers, reviews on modern trends in different fields of microbiological science, and short communications with descriptions of unusual observations. The journal welcomes manuscripts from all countries in the English or Russian language.
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