Analysis of Lsm Protein-Mediated Regulation in the Haloarchaeon <i>Haloferax mediterranei</i>
The Sm protein superfamily includes Sm, like-Sm (Lsm), and Hfq found in the <i>Eukarya</i>, <i>Archaea</i>, and <i>Bacteria</i> domains. Archaeal Lsm proteins have been shown to bind sRNAs and are probably involved in various cellular processes, suggesting a simil...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-01-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/25/1/580 |
| _version_ | 1797358657450541056 |
|---|---|
| author | Gloria Payá Vanesa Bautista Sandra Pastor-Soler Mónica Camacho Julia Esclapez María-José Bonete |
| author_facet | Gloria Payá Vanesa Bautista Sandra Pastor-Soler Mónica Camacho Julia Esclapez María-José Bonete |
| author_sort | Gloria Payá |
| collection | DOAJ |
| description | The Sm protein superfamily includes Sm, like-Sm (Lsm), and Hfq found in the <i>Eukarya</i>, <i>Archaea</i>, and <i>Bacteria</i> domains. Archaeal Lsm proteins have been shown to bind sRNAs and are probably involved in various cellular processes, suggesting a similar function in regulating sRNAs by Hfq in bacteria. Moreover, archaeal Lsm proteins probably represent the ancestral Lsm domain from which eukaryotic Sm proteins have evolved. In this work, <i>Haloferax mediterranei</i> was used as a model organism because it has been widely used to investigate the nitrogen cycle and its regulation in Haloarchaea. Predicting this protein’s secondary and tertiary structures has resulted in a three-dimensional model like the solved Lsm protein structure of <i>Archaeoglobus fulgidus</i>. To obtain information on the oligomerization state of the protein, homologous overexpression and purification by means of molecular exclusion chromatography have been performed. The results show that this protein can form hexameric complexes, which can aggregate into 6 or 12 hexameric rings depending on the NaCl concentration and without RNA. In addition, the study of transcriptional expression via microarrays has allowed us to obtain the target genes regulated by the Lsm protein under nutritional stress conditions: nitrogen or carbon starvation. Microarray analysis has shown the first universal stress proteins (USP) in this microorganism that mediate survival in situations of nitrogen deficiency. |
| first_indexed | 2024-03-08T15:04:35Z |
| format | Article |
| id | doaj.art-49531f3c49654b3ca1d0d5fcf170b601 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-08T15:04:35Z |
| publishDate | 2024-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-49531f3c49654b3ca1d0d5fcf170b6012024-01-10T15:00:05ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672024-01-0125158010.3390/ijms25010580Analysis of Lsm Protein-Mediated Regulation in the Haloarchaeon <i>Haloferax mediterranei</i>Gloria Payá0Vanesa Bautista1Sandra Pastor-Soler2Mónica Camacho3Julia Esclapez4María-José Bonete5Department of Biochemistry and Molecular Biology and Soil Science and Agricultural Chemistry, Faculty of Science, University of Alicante, Ap 99, 03080 Alicante, SpainDepartment of Biochemistry and Molecular Biology and Soil Science and Agricultural Chemistry, Faculty of Science, University of Alicante, Ap 99, 03080 Alicante, SpainDepartment of Biochemistry and Molecular Biology and Soil Science and Agricultural Chemistry, Faculty of Science, University of Alicante, Ap 99, 03080 Alicante, SpainDepartment of Biochemistry and Molecular Biology and Soil Science and Agricultural Chemistry, Faculty of Science, University of Alicante, Ap 99, 03080 Alicante, SpainDepartment of Biochemistry and Molecular Biology and Soil Science and Agricultural Chemistry, Faculty of Science, University of Alicante, Ap 99, 03080 Alicante, SpainDepartment of Biochemistry and Molecular Biology and Soil Science and Agricultural Chemistry, Faculty of Science, University of Alicante, Ap 99, 03080 Alicante, SpainThe Sm protein superfamily includes Sm, like-Sm (Lsm), and Hfq found in the <i>Eukarya</i>, <i>Archaea</i>, and <i>Bacteria</i> domains. Archaeal Lsm proteins have been shown to bind sRNAs and are probably involved in various cellular processes, suggesting a similar function in regulating sRNAs by Hfq in bacteria. Moreover, archaeal Lsm proteins probably represent the ancestral Lsm domain from which eukaryotic Sm proteins have evolved. In this work, <i>Haloferax mediterranei</i> was used as a model organism because it has been widely used to investigate the nitrogen cycle and its regulation in Haloarchaea. Predicting this protein’s secondary and tertiary structures has resulted in a three-dimensional model like the solved Lsm protein structure of <i>Archaeoglobus fulgidus</i>. To obtain information on the oligomerization state of the protein, homologous overexpression and purification by means of molecular exclusion chromatography have been performed. The results show that this protein can form hexameric complexes, which can aggregate into 6 or 12 hexameric rings depending on the NaCl concentration and without RNA. In addition, the study of transcriptional expression via microarrays has allowed us to obtain the target genes regulated by the Lsm protein under nutritional stress conditions: nitrogen or carbon starvation. Microarray analysis has shown the first universal stress proteins (USP) in this microorganism that mediate survival in situations of nitrogen deficiency.https://www.mdpi.com/1422-0067/25/1/580like-Sm proteinsHfqLsmnutritional stress conditionsmicroarray |
| spellingShingle | Gloria Payá Vanesa Bautista Sandra Pastor-Soler Mónica Camacho Julia Esclapez María-José Bonete Analysis of Lsm Protein-Mediated Regulation in the Haloarchaeon <i>Haloferax mediterranei</i> International Journal of Molecular Sciences like-Sm proteins Hfq Lsm nutritional stress conditions microarray |
| title | Analysis of Lsm Protein-Mediated Regulation in the Haloarchaeon <i>Haloferax mediterranei</i> |
| title_full | Analysis of Lsm Protein-Mediated Regulation in the Haloarchaeon <i>Haloferax mediterranei</i> |
| title_fullStr | Analysis of Lsm Protein-Mediated Regulation in the Haloarchaeon <i>Haloferax mediterranei</i> |
| title_full_unstemmed | Analysis of Lsm Protein-Mediated Regulation in the Haloarchaeon <i>Haloferax mediterranei</i> |
| title_short | Analysis of Lsm Protein-Mediated Regulation in the Haloarchaeon <i>Haloferax mediterranei</i> |
| title_sort | analysis of lsm protein mediated regulation in the haloarchaeon i haloferax mediterranei i |
| topic | like-Sm proteins Hfq Lsm nutritional stress conditions microarray |
| url | https://www.mdpi.com/1422-0067/25/1/580 |
| work_keys_str_mv | AT gloriapaya analysisoflsmproteinmediatedregulationinthehaloarchaeonihaloferaxmediterraneii AT vanesabautista analysisoflsmproteinmediatedregulationinthehaloarchaeonihaloferaxmediterraneii AT sandrapastorsoler analysisoflsmproteinmediatedregulationinthehaloarchaeonihaloferaxmediterraneii AT monicacamacho analysisoflsmproteinmediatedregulationinthehaloarchaeonihaloferaxmediterraneii AT juliaesclapez analysisoflsmproteinmediatedregulationinthehaloarchaeonihaloferaxmediterraneii AT mariajosebonete analysisoflsmproteinmediatedregulationinthehaloarchaeonihaloferaxmediterraneii |