Gene Paragraphs at StylonychiaDB

Paragraph NoParagraph TextGene Name
1Histone gene HIS31 encoding histone variant H3.1, formerly H3v3 (before 2013). Renamed with respect to: Talbert PB et al. A unified phylogeny-based nomenclature for histone variants. Epigenetics Chromatin. 2012 Jun 21;5:7. doi: 10.1186/1756-8935-5-7. PubMed PMID: 22650316; PubMed Central PMCID: PMC3380720.HIS31
2Histone gene HIS32 encoding histone variant H3.2, formerly H3v2/v7/v9 (before 2013). Renamed with respect to: Talbert PB et al. A unified phylogeny-based nomenclature for histone variants. Epigenetics Chromatin. 2012 Jun 21;5:7. doi: 10.1186/1756-8935-5-7. PubMed PMID: 22650316; PubMed Central PMCID: PMC3380720. HIS32
3Histone gene HIS33 encoding histone variant H3.3, formerly H3v5 (before 2013). Renamed with respect to: Talbert PB et al. A unified phylogeny-based nomenclature for histone variants. Epigenetics Chromatin. 2012 Jun 21;5:7. doi: 10.1186/1756-8935-5-7. PubMed PMID: 22650316; PubMed Central PMCID: PMC3380720.HIS33
4Possibly 3 paralogs encoding 2 protein variants exist: H3.2a, H3.2b(S29L).HIS32
5Histone gene HIS34 encoding histone variant H3.4, formerly H3v4 (before 2013). Renamed with respect to: Talbert PB et al. A unified phylogeny-based nomenclature for histone variants. Epigenetics Chromatin. 2012 Jun 21;5:7. doi: 10.1186/1756-8935-5-7. PubMed PMID: 22650316; PubMed Central PMCID: PMC3380720. HIS34
6Histone gene HIS35 encoding histone variant H3.5, formerly H3v1 (before 2013). Renamed with respect to: Talbert PB et al. A unified phylogeny-based nomenclature for histone variants. Epigenetics Chromatin. 2012 Jun 21;5:7. doi: 10.1186/1756-8935-5-7. PubMed PMID: 22650316; PubMed Central PMCID: PMC3380720. HIS35
7Histone gene HIS36 encoding histone variant H3.6, formerly H3v8 (before 2013). Renamed with respect to: Talbert PB et al. A unified phylogeny-based nomenclature for histone variants. Epigenetics Chromatin. 2012 Jun 21;5:7. doi: 10.1186/1756-8935-5-7. PubMed PMID: 22650316; PubMed Central PMCID: PMC3380720. HIS36
8Histone gene HIS37 encoding histone variant H3.7, formerly H3v10 (before 2013). Renamed with respect to: Talbert PB et al. A unified phylogeny-based nomenclature for histone variants. Epigenetics Chromatin. 2012 Jun 21;5:7. doi: 10.1186/1756-8935-5-7. PubMed PMID: 22650316; PubMed Central PMCID: PMC3380720. HIS37
9H3.7 is specifically expressed during sexual reproduction of Stylonychia lemnae. Localization of this 20 kDa histone H3 variant is restricted to developing macronuclei (anlagen). HIS37
10Histone gene HIS38 encoding histone variant H3.8, formerly mdp64 (before 2013). Renamed with respect to: Talbert PB et al. A unified phylogeny-based nomenclature for histone variants. Epigenetics Chromatin. 2012 Jun 21;5:7. doi: 10.1186/1756-8935-5-7. PubMed PMID: 22650316; PubMed Central PMCID: PMC3380720. HIS38
11Possibly indentical to protein X (Schlegel et al (1990) Transcriptionally inactive micronuclei, macronuclear anlagen and transcriptionally active macronuclei differ in histone composition in the hypotrichous ciliateStylonychia lemnae. Chromosoma 99(6) 401-406.)HIS38
12Weston R, Peeters H, Ahel D. ZRANB3 is a structure-specific ATP-dependent endonuclease involved in replication stress response. Genes Dev. 2012 Jul 15;26(14):1558-72. doi: 10.1101/gad.193516.112. Epub 2012 Jul 3. PubMed PMID: 22759634; PubMed Central PMCID: PMC3404384.ZRB3
131. Gene. 2012 Apr 15;497(2):147-54. doi: 10.1016/j.gene.2012.01.068. Epub 2012 Feb 2. A telomerase-associated RecQ protein-like helicase resolves telomeric G-quadruplex structures during replication. Postberg J(1), Tsytlonok M, Sparvoli D, Rhodes D, Lipps HJ. Author information: (1)Centre for Biomedical Education and Research, Institute of Cell Biology, Witten, Germany. It is well established that G-quadruplex DNA structures form at ciliate telomeres and their formation throughout the cell-cycle by telomere-end-binding proteins (TEBPs) has been analyzed. During replication telomeric G-quadruplex structure has to be resolved to allow telomere replication by telomerase. It was shown that both phosphorylation of TEBPβ and binding of telomerase are prerequisites for this process, but probably not sufficient to unfold G-quadruplex structure in timely manner to allow replication to proceed. Here we describe a RecQ-like helicase required for unfolding of G-quadruplex structures in vivo. This helicase is highly reminiscent of human RecQ protein-like 4 helicase as well as other RecQ-like helicase found in various eukaryotes and E. coli. In situ analyses combined with specific silencing of either the telomerase or the helicase by RNAi and co-immunoprecipitation experiments demonstrate that this helicase is associated with telomerase during replication and becomes recruited to telomeres by this enzyme. In vitro assays showed that a nuclear extract prepared from cells in S-phase containing both the telomerase as well as the helicase resolves telomeric G-quadruplex structure. This finding can be incorporated into a mechanistic model about the replication of telomeric G-quadruplex structures during the cell cycle. Copyright © 2012 Elsevier B.V. All rights reserved. PMCID: PMC3650557 PMID: 22327026 [PubMed - indexed for MEDLINE]DEAD3