Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle
Histone H1 of most eukaryotes is phosphorylated during the cell cycle progression and seems to play a role in the regulation of chromatin structure, affecting replication and chromosome condensation. In trypanosomatids, histone H1 lacks the globular domain and is shorter when compared with the histo...
| Publicado: |
2005
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v140_n1_p75_DaCunha http://hdl.handle.net/20.500.12110/paper_01666851_v140_n1_p75_DaCunha |
| Aporte de: |
| id |
paper:paper_01666851_v140_n1_p75_DaCunha |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_01666851_v140_n1_p75_DaCunha2023-06-08T15:15:56Z Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle CDK Cell cycle Histone H1 Phosphatase Phosphorylation Trypanosoma cruzi amino acid calyculin A cyclin dependent kinase enzyme histone H1 hydroxyurea lactacystin okadaic acid serine serylprolyllysyllysine unclassified drug amino acid sequence article cell cycle G1 phase cell cycle G2 phase cell cycle S phase cell proliferation enzyme binding mass spectrometry nonhuman nucleotide sequence priority journal protein dephosphorylation protein localization protein phosphorylation Trypanosoma cruzi Eukaryota Trypanosoma Trypanosoma cruzi Trypanosoma cruzi Histone H1 of most eukaryotes is phosphorylated during the cell cycle progression and seems to play a role in the regulation of chromatin structure, affecting replication and chromosome condensation. In trypanosomatids, histone H1 lacks the globular domain and is shorter when compared with the histone of other eukaryotes. We have previously shown that in Trypanosoma cruzi, the agent of Chagas' disease, histone H1 is phosphorylated and this increases its dissociation from chromatin. Here, we demonstrate using mass spectrometry analysis that T. cruzi histone H1 is only phosphorylated at the serine 12 in the sequence SPKK, a typical cyclin-dependent kinase site. We also found a correlation between the phosphorylation state of histone H1 and the cell cycle. Hydroxyurea and lactacystin, which, respectively, arrest parasites at the G1/S and G2/M stages of the cell cycle, increased the level of histone H1 phosphorylation. Cyclin-dependent kinase-related enzymes TzCRK3, and less intensely the TzCRK1 were able to phosphorylate histone H1 in vitro. Histone H1 dephosphorylation was prevented by treating the parasites with okadaic acid but not with calyculin A. These findings suggest that T. cruzi histone H1 phosphorylation is promoted by cyclin dependent kinases, present during S through G2 phase of the cell cycle, and its dephosphorylation is promoted by specific phosphatases. © 2004 Elsevier B.V. All rights reserved. 2005 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v140_n1_p75_DaCunha http://hdl.handle.net/20.500.12110/paper_01666851_v140_n1_p75_DaCunha |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
CDK Cell cycle Histone H1 Phosphatase Phosphorylation Trypanosoma cruzi amino acid calyculin A cyclin dependent kinase enzyme histone H1 hydroxyurea lactacystin okadaic acid serine serylprolyllysyllysine unclassified drug amino acid sequence article cell cycle G1 phase cell cycle G2 phase cell cycle S phase cell proliferation enzyme binding mass spectrometry nonhuman nucleotide sequence priority journal protein dephosphorylation protein localization protein phosphorylation Trypanosoma cruzi Eukaryota Trypanosoma Trypanosoma cruzi Trypanosoma cruzi |
| spellingShingle |
CDK Cell cycle Histone H1 Phosphatase Phosphorylation Trypanosoma cruzi amino acid calyculin A cyclin dependent kinase enzyme histone H1 hydroxyurea lactacystin okadaic acid serine serylprolyllysyllysine unclassified drug amino acid sequence article cell cycle G1 phase cell cycle G2 phase cell cycle S phase cell proliferation enzyme binding mass spectrometry nonhuman nucleotide sequence priority journal protein dephosphorylation protein localization protein phosphorylation Trypanosoma cruzi Eukaryota Trypanosoma Trypanosoma cruzi Trypanosoma cruzi Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle |
| topic_facet |
CDK Cell cycle Histone H1 Phosphatase Phosphorylation Trypanosoma cruzi amino acid calyculin A cyclin dependent kinase enzyme histone H1 hydroxyurea lactacystin okadaic acid serine serylprolyllysyllysine unclassified drug amino acid sequence article cell cycle G1 phase cell cycle G2 phase cell cycle S phase cell proliferation enzyme binding mass spectrometry nonhuman nucleotide sequence priority journal protein dephosphorylation protein localization protein phosphorylation Trypanosoma cruzi Eukaryota Trypanosoma Trypanosoma cruzi Trypanosoma cruzi |
| description |
Histone H1 of most eukaryotes is phosphorylated during the cell cycle progression and seems to play a role in the regulation of chromatin structure, affecting replication and chromosome condensation. In trypanosomatids, histone H1 lacks the globular domain and is shorter when compared with the histone of other eukaryotes. We have previously shown that in Trypanosoma cruzi, the agent of Chagas' disease, histone H1 is phosphorylated and this increases its dissociation from chromatin. Here, we demonstrate using mass spectrometry analysis that T. cruzi histone H1 is only phosphorylated at the serine 12 in the sequence SPKK, a typical cyclin-dependent kinase site. We also found a correlation between the phosphorylation state of histone H1 and the cell cycle. Hydroxyurea and lactacystin, which, respectively, arrest parasites at the G1/S and G2/M stages of the cell cycle, increased the level of histone H1 phosphorylation. Cyclin-dependent kinase-related enzymes TzCRK3, and less intensely the TzCRK1 were able to phosphorylate histone H1 in vitro. Histone H1 dephosphorylation was prevented by treating the parasites with okadaic acid but not with calyculin A. These findings suggest that T. cruzi histone H1 phosphorylation is promoted by cyclin dependent kinases, present during S through G2 phase of the cell cycle, and its dephosphorylation is promoted by specific phosphatases. © 2004 Elsevier B.V. All rights reserved. |
| title |
Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle |
| title_short |
Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle |
| title_full |
Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle |
| title_fullStr |
Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle |
| title_full_unstemmed |
Trypanosoma cruzi histone H1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle |
| title_sort |
trypanosoma cruzi histone h1 is phosphorylated in a typical cyclin dependent kinase site accordingly to the cell cycle |
| publishDate |
2005 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v140_n1_p75_DaCunha http://hdl.handle.net/20.500.12110/paper_01666851_v140_n1_p75_DaCunha |
| _version_ |
1768542122073391104 |