Nucleus-specific linker histones Hho1 and Mlh1 form distinct protein interactions during growth, starvation and development in Tetrahymena thermophila
| Autor: | Joanna Derynck, Alejandro Saettone, Jean-Philippe Lambert, Jeffrey Fillingham, Ronald E. Pearlman, Jyoti Garg, Kanwal Ashraf, Syed Nabeel-Shah |
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| Rok vydání: | 2020 |
| Předmět: |
Proteomics
0301 basic medicine Proteome Protozoan Proteins lcsh:Medicine Article Tetrahymena thermophila Protein–protein interaction Histones 03 medical and health sciences Histone H1 Animals Protein Interaction Domains and Motifs Amino Acid Sequence lcsh:Science Cell Nucleus Regulation of gene expression Multidisciplinary 030102 biochemistry & molecular biology biology Chemistry lcsh:R High Mobility Group Proteins Tetrahymena Gene Expression Regulation Developmental biology.organism_classification Chromatin Cell biology 030104 developmental biology Histone Gene Expression Regulation Starvation biology.protein lcsh:Q Epigenetics MutL Protein Homolog 1 Linker Post-translational modifications |
| Zdroj: | Scientific Reports Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020) |
| ISSN: | 2045-2322 |
| Popis: | Chromatin organization influences most aspects of gene expression regulation. The linker histone H1, along with the core histones, is a key component of eukaryotic chromatin. Despite its critical roles in chromatin structure and function and gene regulation, studies regarding the H1 protein-protein interaction networks, particularly outside of Opisthokonts, are limited. The nuclear dimorphic ciliate protozoan Tetrahymena thermophila encodes two distinct nucleus-specific linker histones, macronuclear Hho1 and micronuclear Mlh1. We used a comparative proteomics approach to identify the Hho1 and Mlh1 protein-protein interaction networks in Tetrahymena during growth, starvation, and sexual development. Affinity purification followed by mass spectrometry analysis of the Hho1 and Mlh1 proteins revealed a non-overlapping set of co-purifying proteins suggesting that Tetrahymena nucleus-specific linker histones are subject to distinct regulatory pathways. Furthermore, we found that linker histones interact with distinct proteins under the different stages of the Tetrahymena life cycle. Hho1 and Mlh1 co-purified with several Tetrahymena-specific as well as conserved interacting partners involved in chromatin structure and function and other important cellular pathways. Our results suggest that nucleus-specific linker histones might be subject to nucleus-specific regulatory pathways and are dynamically regulated under different stages of the Tetrahymena life cycle. |
| Databáze: | OpenAIRE |
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