Identification and functional analysis of the mitochondrial cysteine synthase TtCsa2 from Tetrahymena thermophila

2021 ◽  
Author(s):  
Hongrui Lv ◽  
Lina Hu ◽  
Jing Xu ◽  
Tao Bo ◽  
Wei Wang
Keyword(s):  
Functional Analysis ◽  
Tetrahymena Thermophila ◽  
Cysteine Synthase

scholarly journals Functional analysis of the methyltransferase SMYD in the single-cell model organism Tetrahymena thermophila

2020 ◽  
Vol 2 (2) ◽  
pp. 109-122
Author(s):  
Xiaolu Zhao ◽  
Yuan Li ◽  
Lili Duan ◽  
Xiao Chen ◽  
Fengbiao Mao ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Single Cell ◽  
Tetrahymena Thermophila ◽  
Cell Model ◽  
Model Organism ◽  
Single Cell Model

scholarly journals Functional analysis of chromatin assembly genes in tetrahymena thermophila

2021 ◽  
Author(s):  
Renu Jeyapala
Keyword(s):  
Functional Analysis ◽  
Tetrahymena Thermophila ◽  
Histone Variants ◽  
Chromatin Assembly ◽  
Base Pairs ◽  
Post Translational Modifications ◽  
Disease States ◽  
Core Histones ◽  
Chromatin Biology ◽  
Assembly Pathways

The basic structural unit of chromatin is the nucleosome composed of ~147 base pairs of DNA wrapped around an octamer of histone proteins. Post-translational modifications such as histone acetylation or the substitution of histone variants in place of core histones have been implicated in various chromatin related processes. There are two distinct chromatin assembly pathways. Replication-dependent mediated by CAF-1 (H3-H4) and replication-independent mediated by HIRA (H3.3-H4). Miss-regulation of chromatin assembly patterns result in the onset of many disease states such as cancer. Tetrahymena thermophila is a useful model for understanding basic questions in chromatin biology due to the segregation of transcriptionally active and silent chromatin into two distinct nuclei. To better characterize replication-dependent and independent chromatin assembly pathways in T. thermophila, I have engineered somatic knockouts (HIRA, CAC2, UBN1 and UBN2) and initiated the functional analysis of these chromatin assembly genes mediated in growth and development. The absence of CAC2 results in larger macronuclei and speculated to be a result of reduced histone H3-H4 deposition onto chromatin during growth.

scholarly journals Functional analysis of chromatin assembly genes in tetrahymena thermophila

2021 ◽  
Author(s):  
Renu Jeyapala
Keyword(s):  
Functional Analysis ◽  
Tetrahymena Thermophila ◽  
Histone Variants ◽  
Chromatin Assembly ◽  
Base Pairs ◽  
Post Translational Modifications ◽  
Disease States ◽  
Core Histones ◽  
Chromatin Biology ◽  
Assembly Pathways

The basic structural unit of chromatin is the nucleosome composed of ~147 base pairs of DNA wrapped around an octamer of histone proteins. Post-translational modifications such as histone acetylation or the substitution of histone variants in place of core histones have been implicated in various chromatin related processes. There are two distinct chromatin assembly pathways. Replication-dependent mediated by CAF-1 (H3-H4) and replication-independent mediated by HIRA (H3.3-H4). Miss-regulation of chromatin assembly patterns result in the onset of many disease states such as cancer. Tetrahymena thermophila is a useful model for understanding basic questions in chromatin biology due to the segregation of transcriptionally active and silent chromatin into two distinct nuclei. To better characterize replication-dependent and independent chromatin assembly pathways in T. thermophila, I have engineered somatic knockouts (HIRA, CAC2, UBN1 and UBN2) and initiated the functional analysis of these chromatin assembly genes mediated in growth and development. The absence of CAC2 results in larger macronuclei and speculated to be a result of reduced histone H3-H4 deposition onto chromatin during growth.

scholarly journals The LisH Domain-Containing N-Terminal Fragment is Important for the Localization, Dimerization, and Stability of Katnal2 in Tetrahymena

Cells ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 292
Author(s):  
Ewa Joachimiak ◽  
Ewa Waclawek ◽  
Michal Niziolek ◽  
Anna Osinka ◽  
Hanna Fabczak ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Catalytic Domain ◽  
Tetrahymena Thermophila ◽  
Basal Bodies ◽  
Amino Acid Sequence Homology ◽  
Terminal Fragment ◽  
Wide Range ◽  
Microtubular Structures

Katanin-like 2 protein (Katnal2) orthologs have a tripartite domain organization. Two highly conserved regions, an N-terminal LisH (Lis-homology) domain and a C-terminal AAA catalytic domain, are separated by a less conserved linker. The AAA domain of Katnal2 shares the highest amino acid sequence homology with the AAA domain of the canonical katanin p60. Katnal2 orthologs are present in a wide range of eukaryotes, from protists to humans. In the ciliate Tetrahymena thermophila, a Katnal2 ortholog, Kat2, co-localizes with the microtubular structures, including basal bodies and ciliary outer doublets, and this co-localization is sensitive to levels of microtubule glutamylation. The functional analysis of Kat2 domains suggests that an N-terminal fragment containing a LisH domain plays a role in the subcellular localization, dimerization, and stability of Kat2.

Functional analysis of metallothionein MTT5 from Tetrahymena thermophila

2018 ◽  
Vol 119 (4) ◽  
pp. 3257-3266 ◽  
Author(s):  
Huanxin Zhou ◽  
Jing Xu ◽  
Wei Wang
Keyword(s):  
Functional Analysis ◽  
Tetrahymena Thermophila
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