Nucleus-specific linker histones Hho1 and Mlh1 form distinct protein interactions during growth, starvation and development in Tetrahymena thermophila - Nabeel-Shah, Syed; Ashraf, Kanwal; Saettone, Alejandro; Garg, Jyoti; Derynck, Joanna; Lambert, Jean-Philippe; Pearlman, Ronald E.; Fillingham, Jeffrey (Scientific reports, 2020)
Keywords: 631/337/100; 631/337/176; 631/337/458; 631/337/475; Amino Acid Sequence; Animals; Cell Nucleus - genetics; Cell Nucleus - metabolism; Chromatin; Chromatin - genetics; Chromatin - metabolism; Gene expression; Gene Expression Regulation; Gene Expression Regulation, Developmental; Gene regulation; High Mobility Group Proteins - genetics; High Mobility Group Proteins - metabolism; Histone H1; Histones - metabolism; Humanities and Social Sciences; Life cycles; Mass spectrometry; Mass spectroscopy; MLH1 protein; multidisciplinary; MutL Protein Homolog 1 - genetics; MutL Protein Homolog 1 - metabolism; Protein interaction; Protein Interaction Domains and Motifs; Protein purification; Proteins; Proteome - analysis; Proteomics; Protozoa; Protozoan Proteins - genetics; Protozoan Proteins - metabolism; Science; Science (multidisciplinary); Starvation; Structure-function relationships; Tetrahymena; Tetrahymena thermophila; Tetrahymena thermophila - genetics; Tetrahymena thermophila - growth & development; Tetrahymena thermophila - metabolism