Regulation of the expression of histone H3.3 by differential polyadenylation

Genome ◽  
2005 ◽  
Vol 48 (3) ◽  
pp. 503-510 ◽  
Author(s):  
Rongrong Feng ◽  
Xiaoying Tang ◽  
Angela Becker ◽  
Anja Berger ◽  
Jing Ye ◽  
...  

Previously we have shown that the 3' untranslated regions (UTRs) of the replacement histone genes H3.3.A and H3.3B of Drosophila melanogaster differ in their nucleotide sequences and have different polyadenylation sites. To understand their functional relevance, which might explain the presence and evolutionary conservation of 2 different H3.3 genes, green flourescent protein (GFP) constructs with different 3' UTR sections were studied by the expression of GFP as a marker protein. Here we show that the polyadenylation signals modify the cell-specific translation of the histone replacement variants in testes and ovaries. The H3.3A gene may be required to provide postmeiotic histone H3.3 in the male germ line in transition to chromatin packaging in sperm.Key words: histone H3.3, polyadenylation, oogenesis, spermatogenesis, histone translation.

2020 ◽  
Vol 49 (D1) ◽  
pp. D47-D54
Author(s):  
Weiwei Jin ◽  
Qizhao Zhu ◽  
Yanbo Yang ◽  
Wenqian Yang ◽  
Dongyang Wang ◽  
...  

Abstract Alternative polyadenylation (APA) is an important post-transcriptional regulatory mechanism that recognizes different polyadenylation signals on transcripts, resulting in transcripts with different lengths of 3′ untranslated regions and thereby influencing a series of biological processes. Recent studies have highlighted the important roles of APA in human. However, APA profiles in other animals have not been fully recognized, and there is no database that provides comprehensive APA information for other animals except human. Here, by using the RNA sequencing data collected from public databases, we systematically characterized the APA profiles in 9244 samples of 18 species. In total, we identified 342 952 APA events with a median of 17 020 per species using the DaPars2 algorithm, and 315 691 APA events with a median of 17 953 per species using the QAPA algorithm in these 18 species, respectively. In addition, we predicted the polyadenylation sites (PAS) and motifs near PAS of these species. We further developed Animal-APAdb, a user-friendly database (http://gong_lab.hzau.edu.cn/Animal-APAdb/) for data searching, browsing and downloading. With comprehensive information of APA events in different tissues of different species, Animal-APAdb may greatly facilitate the exploration of animal APA patterns and novel mechanisms, gene expression regulation and APA evolution across tissues and species.


2008 ◽  
Vol 86 (5) ◽  
pp. 380-385 ◽  
Author(s):  
Alexandra Weyrich ◽  
Xiaojing Tang ◽  
Guoliang Xu ◽  
André Schrattenholz ◽  
Christian Hunzinger ◽  
...  

It is controversial whether DNA methylation plays a functional role in Drosophila . We have studied testis DNA of Drosophila melanogaster Meigen, 1830 with antisera against 5-methylcytosine (5mC) and found no evidence for the presence of significant amounts of 5mC. Reactions occur only with 1 of 3 5mC antisera, but they are restricted to nuclear regions without detectable amounts of DNA. The antisera apparently cross-react with other nuclear components. If the murine de novo DNA methyltransferases, DNMT3A and DNMT3B, are expressed under the control of the spermatocyte-specific β2-tubulin promoter in testes, DNA methylation is not increased and no effects on the fertility of the fly are seen. DNA methylation has, therefore, no functional relevance in the male germ line of Drosophila.


2006 ◽  
Author(s):  
Laura K. Braydich-Stolle ◽  
Saber Hussain ◽  
John J. Schlager ◽  
Marie-Claude Hofmann

Chromosoma ◽  
1999 ◽  
Vol 108 (4) ◽  
pp. 235-242 ◽  
Author(s):  
Harry R. Harhangi ◽  
Xiaoping Sun ◽  
Ya Xian Wang ◽  
Anna Akhmanova ◽  
Koos Miedema ◽  
...  

1993 ◽  
Vol 292 (2) ◽  
pp. 343-349 ◽  
Author(s):  
R Y Y Chan ◽  
H M Schulman ◽  
P Ponka

Ferrochelatase, which catalyses the last step in haem biosynthesis, i.e. the insertion of Fe(II) into protophorphyrin IX, is present in all cells, but is particularly abundant in erythroid cells during haemoglobinization. Using mouse ferrochelatase cDNA as a probe two ferrochelatase transcripts, having lengths of 2.9 kb and 2.2 kb, were found in extracts of mouse liver, kidney, brain, muscle and spleen, the 2.9 kb transcript being more abundant in the non-erythroid tissues and the 2.2 kb transcript more predominant in spleen. In mouse erythroleukemia cells the 2.9 kb ferrochelatase transcript is also more abundant; however, following induction of erythroid differentiation by dimethyl sulphoxide there is a preferential increase in the 2.2 kb transcript, which eventually predominates. With mouse reticulocytes, the purest immature erythroid cell population available, over 90% of the total ferrochelatase mRNA is present as the 2.2 kb transcript. Since there is probably only one mouse ferrochelatase gene, the occurrence of two ferrochelatase transcripts could arise from the use of two putative polyadenylation signals in the 3′ region of ferrochelatase DNA. This possibility was explored by using a 389 bp DNA fragment produced by PCR with synthetic oligoprimers having sequence similarity with a region between the polyadenylation sites. This fragment hybridized only to the 2.9 kb ferrochelatase transcript, indicating that the two transcripts differ at their 3′ ends and suggesting that the 2.2 kb transcript results from the utilization of the upstream polyadenylation signal. The preferential utilization of the upstream polyadenylation signal may be an erythroid-specific characteristic of ferrochelatase gene expression.


Genetics ◽  
1994 ◽  
Vol 138 (4) ◽  
pp. 1163-1170 ◽  
Author(s):  
E Wojcik ◽  
A M Murphy ◽  
H Fares ◽  
K Dang-Vu ◽  
S I Tsubota

Abstract A hybrid dysgenesis-induced mutation, enhancer of rudimentaryp1 (e(r)p1), is a recessive enhancer of a weak rudimentary mutant phenotype in Drosophila melanogaster. The e(r) gene was cloned using P element tagging and localized to region 8B on the X chromosome. It encodes a 1.0-kb and a 1.2-kb transcript. The 1.0-kb transcript is present in both adult males and females, while the 1.2-kb transcript is predominantly found in females. The difference in the lengths of the two e(r) transcripts is caused by two different polyadenylation sites spaced 228 bp apart. The amounts of both of these transcripts are drastically reduced in the e(r)p1 mutant. The P element in e(r)p1 is inserted in the 5'-untranslated leader region near the start of transcription. It may be producing its effect by suppressing transcription and/or by providing transcription termination and polyadenylation signals. The putative e(r) protein is 104 amino acids in length and bears no striking resemblance to protein sequences in GenBank or PIR. While its biochemical function is unknown at this time, sequence analysis indicates that the e(r) protein is highly conserved and, presumably, functionally very important. The amino acid sequences of the D. melanogaster and the Drosophila virilis proteins are 95% identical.


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