A novel mode of histone-like protein HupB regulating Sinorhizobium meliloti cell division through lysine acetylation
HU, a small, basic histone-like protein, binds to bacterial genomic DNA, influencing DNA conformation, replication, and transcription. Its acetylation is a key post-translational modification affecting its DNA-binding activity. The role of HU acetylation in regulating cell division through the cell...
Saved in:
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2025-01-01
|
| Series: | Current Research in Microbial Sciences |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2666517425000070 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832586189829308416 |
|---|---|
| author | Ningning Li Huibo Jin Hongbo Li Huilin Yu Xiaoxu Wu Tianci Zhang Liangliang Yu Zhaoling Qin Li Luo |
| author_facet | Ningning Li Huibo Jin Hongbo Li Huilin Yu Xiaoxu Wu Tianci Zhang Liangliang Yu Zhaoling Qin Li Luo |
| author_sort | Ningning Li |
| collection | DOAJ |
| description | HU, a small, basic histone-like protein, binds to bacterial genomic DNA, influencing DNA conformation, replication, and transcription. Its acetylation is a key post-translational modification affecting its DNA-binding activity. The role of HU acetylation in regulating cell division through the cell cycle regulatory system remained largely unknown. In this study, we find that stimulation of lysine acetylation or non-acetylation in HupB, a homolog of HU, differentially regulates the expression of cell cycle regulators, as well as cell growth and division in Sinorhizobium meliloti. Lys3, Lys13, and Lys83 in HupB were identified as acetylated residues by mass spectrometry. Mutating these residues to arginine (stimulating non-acetylation) in HupB impedes normal cell division, while substituting them with glycine (mimicking acetylation) allows for rapid cell duplication. The mimicry of non-acetylated HupB leads to enlarged abnormal cells, while stimulating acetylated HupB only reduces cell length. Transcription activation was observed in the mutant cells. Cell cycle regulators such as CtrA, GcrA and DnaA were differentially expressed in the mutants. HupB substitutions differentially bound to these cell cycle regulatory genes. These findings suggest that the appropriate acetylation of HupB regulates the expression of cell cycle regulators, thereby controlling S. meliloti cell division. |
| format | Article |
| id | doaj-art-3e6372ae33f5475e815059553c2c8cf8 |
| institution | Kabale University |
| issn | 2666-5174 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Current Research in Microbial Sciences |
| spelling | doaj-art-3e6372ae33f5475e815059553c2c8cf82025-01-26T05:05:06ZengElsevierCurrent Research in Microbial Sciences2666-51742025-01-018100345A novel mode of histone-like protein HupB regulating Sinorhizobium meliloti cell division through lysine acetylationNingning Li0Huibo Jin1Hongbo Li2Huilin Yu3Xiaoxu Wu4Tianci Zhang5Liangliang Yu6Zhaoling Qin7Li Luo8Shanghai Key Laboratory of Bio-energy Crops, Center of Plant Science, School of Life Sciences, Shanghai University, Shanghai 200444, ChinaShanghai Key Laboratory of Bio-energy Crops, Center of Plant Science, School of Life Sciences, Shanghai University, Shanghai 200444, ChinaShanghai Key Laboratory of Bio-energy Crops, Center of Plant Science, School of Life Sciences, Shanghai University, Shanghai 200444, ChinaShanghai Key Laboratory of Bio-energy Crops, Center of Plant Science, School of Life Sciences, Shanghai University, Shanghai 200444, ChinaShanghai Key Laboratory of Bio-energy Crops, Center of Plant Science, School of Life Sciences, Shanghai University, Shanghai 200444, ChinaShanghai Key Laboratory of Bio-energy Crops, Center of Plant Science, School of Life Sciences, Shanghai University, Shanghai 200444, ChinaShanghai Key Laboratory of Bio-energy Crops, Center of Plant Science, School of Life Sciences, Shanghai University, Shanghai 200444, ChinaDepartment of Microbiology, Naval Medical University, Shanghai 200433, ChinaShanghai Key Laboratory of Bio-energy Crops, Center of Plant Science, School of Life Sciences, Shanghai University, Shanghai 200444, China; Corresponding author.HU, a small, basic histone-like protein, binds to bacterial genomic DNA, influencing DNA conformation, replication, and transcription. Its acetylation is a key post-translational modification affecting its DNA-binding activity. The role of HU acetylation in regulating cell division through the cell cycle regulatory system remained largely unknown. In this study, we find that stimulation of lysine acetylation or non-acetylation in HupB, a homolog of HU, differentially regulates the expression of cell cycle regulators, as well as cell growth and division in Sinorhizobium meliloti. Lys3, Lys13, and Lys83 in HupB were identified as acetylated residues by mass spectrometry. Mutating these residues to arginine (stimulating non-acetylation) in HupB impedes normal cell division, while substituting them with glycine (mimicking acetylation) allows for rapid cell duplication. The mimicry of non-acetylated HupB leads to enlarged abnormal cells, while stimulating acetylated HupB only reduces cell length. Transcription activation was observed in the mutant cells. Cell cycle regulators such as CtrA, GcrA and DnaA were differentially expressed in the mutants. HupB substitutions differentially bound to these cell cycle regulatory genes. These findings suggest that the appropriate acetylation of HupB regulates the expression of cell cycle regulators, thereby controlling S. meliloti cell division.http://www.sciencedirect.com/science/article/pii/S2666517425000070HUAcetylationLysineCell divisionTranscriptional regulation |
| spellingShingle | Ningning Li Huibo Jin Hongbo Li Huilin Yu Xiaoxu Wu Tianci Zhang Liangliang Yu Zhaoling Qin Li Luo A novel mode of histone-like protein HupB regulating Sinorhizobium meliloti cell division through lysine acetylation Current Research in Microbial Sciences HU Acetylation Lysine Cell division Transcriptional regulation |
| title | A novel mode of histone-like protein HupB regulating Sinorhizobium meliloti cell division through lysine acetylation |
| title_full | A novel mode of histone-like protein HupB regulating Sinorhizobium meliloti cell division through lysine acetylation |
| title_fullStr | A novel mode of histone-like protein HupB regulating Sinorhizobium meliloti cell division through lysine acetylation |
| title_full_unstemmed | A novel mode of histone-like protein HupB regulating Sinorhizobium meliloti cell division through lysine acetylation |
| title_short | A novel mode of histone-like protein HupB regulating Sinorhizobium meliloti cell division through lysine acetylation |
| title_sort | novel mode of histone like protein hupb regulating sinorhizobium meliloti cell division through lysine acetylation |
| topic | HU Acetylation Lysine Cell division Transcriptional regulation |
| url | http://www.sciencedirect.com/science/article/pii/S2666517425000070 |
| work_keys_str_mv | AT ningningli anovelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT huibojin anovelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT hongboli anovelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT huilinyu anovelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT xiaoxuwu anovelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT tiancizhang anovelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT liangliangyu anovelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT zhaolingqin anovelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT liluo anovelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT ningningli novelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT huibojin novelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT hongboli novelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT huilinyu novelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT xiaoxuwu novelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT tiancizhang novelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT liangliangyu novelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT zhaolingqin novelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation AT liluo novelmodeofhistonelikeproteinhupbregulatingsinorhizobiummeliloticelldivisionthroughlysineacetylation |