Nabeel-Shah S, Garg J, Kougnassoukou Tchara PE, Pearlman RE, Lambert JP, Fillingham J (2021) Functional proteomics protocol for the identification of interaction partners in Tetrahymena thermophila. STAR protocols 2(1):100362 PUBMED:33786459
Tian M, Agreiter C, Loidl J (2020) Spatial constraints on chromosomes are instrumental to meiotic pairing. Journal of cell science 133(22): PUBMED:33172984
Nabeel-Shah S, Ashraf K, Saettone A, Garg J, Derynck J, Lambert JP, Pearlman RE, Fillingham J (2020) Nucleus-specific linker histones Hho1 and Mlh1 form distinct protein interactions during growth, starvation and development in Tetrahymena thermophila. Scientific reports 10(1):168 PUBMED:31932604
HTA2 histone H2B.1; Histone H2A; one of the four histones (H2A- H2B- H3 and H4) that comprise the nucleosome core; one of two major histone H2A genes (with HTA1); knockout viable- but double knockout with HTA1 inviable
HTA1 Histone H2A, core histone
protein required for chromati
n assembly and chromosome func
tion; one of two nearly identi
cal subtypes (see also HTA2);
DNA damage-dependent phosphory
lation by Mec1p facilitates DN
A repair; acetylated by Nat4p
Ref:12665578: Ren Q, Gorovsky MA (2003) The nonessential H2A N-terminal tail can function as an essential charge patch on the H2A.Z variant N-terminal tail. Molecular and cellular biology 23(8):2778-89
Ref:11000274: Jackson JD, Gorovsky MA (2000) Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants. Nucleic acids research 28(19):3811-6
Ref:10385122: Clarkson MJ, Wells JR, Gibson F, Saint R, Tremethick DJ (1999) Regions of variant histone His2AvD required for Drosophila development. Nature 399(6737):694-7
Ref:8760889: Liu X, Gorovsky MA (1996) Cloning and characterization of the major histone H2A genes completes the cloning and sequencing of known histone genes of Tetrahymena thermophila. Nucleic acids research 24(15):3023-30
Ref:8649398: Liu X, Bowen J, Gorovsky MA (1996) Either of the major H2A genes but not an evolutionarily conserved H2A.F/Z variant of Tetrahymena thermophila can function as the sole H2A gene in the yeast Saccharomyces cerevisiae. Molecular and cellular biology 16(6):2878-87
Ref:8754831: Liu X, Li B, GorovskyMA (1996) Essential and nonessential histone H2A variants in Tetrahymena thermophila. Molecular and cellular biology 16(8):4305-11
Ref:8177745: Liu X, Gorovsky MA (1993) Mapping the 5' and 3' ends of Tetrahymena thermophila mRNAs using RNA ligase mediated amplification of cDNA ends (RLM-RACE). Nucleic acids research 21(21):4954-60
Ref:2587254: Mannironi C, Bonner WM, Hatch CL (1989) H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3' processing signals. Nucleic acids research 17(22):9113-26
Ref:3131141: Brandt WF, de Andrade Rodrigues J, von Holt C (1988) The amino acid sequence of wheat histone H2B(2). A core histone with a novel repetitive N-terminal extension. European journal of biochemistry 173(3):547-54
Ref:6706903: Fusauchi Y, Iwai K (1984) Tetrahymena histone H2A. Acetylation in the N-terminal sequence and phosphorylation in the C-terminal sequence. Journal of biochemistry 95(1):147-54
Ref:6885734: Fusauchi Y, Iwai K (1983) Tetrahymena histone H2A. Isolation and two variant sequences. Journal of biochemistry 93(6):1487-97