scholarly journals An unusually simple HP1 gene set in Hymenopteran insects

2015 ◽  
Vol 93 (6) ◽  
pp. 596-603 ◽  
Author(s):  
C. Fang ◽  
L. Schmitz ◽  
P.M. Ferree
Keyword(s):  
Gene Family ◽  
Germ Line ◽  
Drosophila Species ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Insect Order ◽  
Representative Species ◽  
Somatic Tissues ◽  
Group A ◽  
Heterochromatin Structure

The heterochromatin protein 1 (HP1) gene family includes a set of paralogs in higher eukaryotes that serve fundamental roles in heterochromatin structure and maintenance, and other chromatin-related functions. At least 10 full and 16 partial HP1 genes exist among Drosophila species, with multiple gene gains, losses, and sub-functionalizations within this insect group. An important question is whether this diverse set of HP1 genes and their dynamic evolution represent the standard rule in eukaryotic groups. Here we have begun to address this question by bio-informatically identifying the HP1 family genes in representative species of the insect order Hymenoptera, which includes all ants, bees, wasps, and sawflies. Compared to Drosophila species, Hymenopterans have a much simpler set of HP1 genes, including one full and two partial HP1s. All 3 genes appear to have been present in the common ancestor of the Hymenopterans and they derive from a Drosophila HP1B-like gene. In ants, a partial HP1 gene containing only a chromoshadow domain harbors amino acid changes at highly conserved sites within the PxVxL recognition region, suggesting that this gene has undergone sub-functionalization. In the jewel wasp Nasonia vitripennis, the full HP1 and partial chromoshadow-only HP1 are expressed in both germ line and somatic tissues. However, the partial chromodomain-only HP1 is expressed exclusively in the ovary and testis, suggesting that it may have a specialized chromatin role during gametogenesis. Our findings demonstrate that the HP1 gene family is much simpler and evolutionarily less dynamic within the Hymenopterans compared to the much younger Drosophila group, a pattern that may reflect major differences in the range of chromatin-related functions present in these and perhaps other insect groups.

scholarly journals Pericentromeric Heterochromatin Domains Are Maintained without Accumulation of HP1

2007 ◽  
Vol 18 (4) ◽  
pp. 1464-1471 ◽  
Author(s):  
Julio Mateos-Langerak ◽  
Maartje C. Brink ◽  
Martijn S. Luijsterburg ◽  
Ineke van der Kraan ◽  
Roel van Driel ◽  
...  
Keyword(s):  
Histone H3 ◽  
Dominant Negative ◽  
Pericentromeric Heterochromatin ◽  
Heterochromatin Protein 1 ◽  
Dapi Staining ◽  
Heterochromatin Protein ◽  
3T3 Fibroblasts ◽  
Heterochromatin Structure ◽  
Hp1 Proteins

The heterochromatin protein 1 (HP1) family is thought to be an important structural component of heterochromatin. HP1 proteins bind via their chromodomain to nucleosomes methylated at lysine 9 of histone H3 (H3K9me). To investigate the role of HP1 in maintaining heterochromatin structure, we used a dominant negative approach by expressing truncated HP1α or HP1β proteins lacking a functional chromodomain. Expression of these truncated HP1 proteins individually or in combination resulted in a strong reduction of the accumulation of HP1α, HP1β, and HP1γ in pericentromeric heterochromatin domains in mouse 3T3 fibroblasts. The expression levels of HP1 did not change. The apparent displacement of HP1α, HP1β, and HP1γ from pericentromeric heterochromatin did not result in visible changes in the structure of pericentromeric heterochromatin domains, as visualized by DAPI staining and immunofluorescent labeling of H3K9me. Our results show that the accumulation of HP1α, HP1β, and HP1γ at pericentromeric heterochromatin domains is not required to maintain DAPI-stained pericentromeric heterochromatin domains and the methylated state of histone H3 at lysine 9 in such heterochromatin domains.

Developmental-stage-specific expression of the hsp70 gene family during differentiation of the mammalian male germ line

1987 ◽  
Vol 7 (5) ◽  
pp. 1791-1796
Author(s):  
Z F Zakeri ◽  
D J Wolgemuth
Keyword(s):  
Heat Shock ◽  
Gene Family ◽  
Germ Line ◽  
Cell Lineage ◽  
Hsp70 Gene ◽  
Developmentally Regulated ◽  
Specific Expression ◽  
Hsp70 Mrna ◽  
Somatic Tissues ◽  
Exogenous Stress

Mouse somatic tissues contain low levels of transcripts homologous to the heat shock-inducible and cognate members of the heat shock protein 70 (hsp70) gene family. An abundant, unique sized hsp70 mRNA of 2.7 kilobases (kb) is present in testes in the absence of exogenous stress. Its expression is restricted to germ cells and is developmentally regulated. The 2.7-kb transcript first appears during the haploid phase of spermatogenesis and is stable throughout the morphogenic stages of spermiogenesis. A 2.7-kb hsp70 mRNA is present in rat and human testes. These observations suggest that a member of the hsp70 gene family plays a role in the development of the mammalian male germ cell lineage.

scholarly journals Rapid evolution of a Y-chromosome heterochromatin protein underlies sex chromosome meiotic drive

2016 ◽  
Vol 113 (15) ◽  
pp. 4110-4115 ◽  
Author(s):  
Quentin Helleu ◽  
Pierre R. Gérard ◽  
Raphaëlle Dubruille ◽  
David Ogereau ◽  
Benjamin Prud’homme ◽  
...  
Keyword(s):  
Sex Ratio ◽  
Y Chromosome ◽  
Sex Chromosome ◽  
Rapid Evolution ◽  
Meiotic Drive ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Intragenomic Conflict ◽  
Heterochromatin Structure ◽  
Evolutionary Consequences

Sex chromosome meiotic drive, the non-Mendelian transmission of sex chromosomes, is the expression of an intragenomic conflict that can have extreme evolutionary consequences. However, the molecular bases of such conflicts remain poorly understood. Here, we show that a young and rapidly evolving X-linked heterochromatin protein 1 (HP1) gene, HP1D2, plays a key role in the classical Paris sex-ratio (SR) meiotic drive occurring in Drosophila simulans. Driver HP1D2 alleles prevent the segregation of the Y chromatids during meiosis II, causing female-biased sex ratio in progeny. HP1D2 accumulates on the heterochromatic Y chromosome in male germ cells, strongly suggesting that it controls the segregation of sister chromatids through heterochromatin modification. We show that Paris SR drive is a consequence of dysfunctional HP1D2 alleles that fail to prepare the Y chromosome for meiosis, thus providing evidence that the rapid evolution of genes controlling the heterochromatin structure can be a significant source of intragenomic conflicts.

scholarly journals Structural studies of Rhino protein in piRNA biogenesis

2014 ◽  
Vol 70 (a1) ◽  
pp. C1589-C1589
Author(s):  
Ying Huang ◽  
Bowen Yu
Keyword(s):  
Small Rna ◽  
Germ Line ◽  
Complex Form ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Ping Pong ◽  
Long Time ◽  
The Difference ◽  
Rna Pathways ◽  
Hp1 Proteins

Small-RNA-guided gene regulation is a common biological process in eukaryotic cells. Animal germ cells are characterized by an intriguing small-RNA-mediated gene-silencing mechanism known as PIWI pathway. PIWI-interacting RNAs (piRNAs) are small, 21-30 nt single-stranded RNAs that associate with PIWI proteins. The function of piRNA is silencing transposon elements in germ line cells to keep the genome integrity since germ line cells are the only source for transmitting genetic information to the next generation. For a long time the biogenesis of piRNA and the mechanism of how it functions remains unclear. The biogenesis of piRNAs is quite different from that of other small-RNA pathways, which is independent of Dicer. piRNA biogenesis occurs through both primary and secondary pathway (or called ping-pong cycle). In drosophila transcripts from heterochromatic clusters are processed into primary piRNAs. A particularly fast evolving homologue of heterochromatin protein 1 (HP1) called Rhino binds to dual-strand piRNA clusters and is required for their production. But how does Rhino recognize histone H3 trimethylated on lysine 9? What's the difference between Rhino and other HP1 proteins? Here we show the crystal structure of Rhino both in apo form and complex form with H3K9me3. We observed a unique dimer interface in Rhino and a domain-swapping in conformational change. These findings provide insights into the molecular mechanism of the specificity of Rhino recognizing histone H3K9me3 and its function in piRNA biogenesis.

scholarly journals Developmental-stage-specific expression of the hsp70 gene family during differentiation of the mammalian male germ line.

1987 ◽  
Vol 7 (5) ◽  
pp. 1791-1796 ◽  
Author(s):  
Z F Zakeri ◽  
D J Wolgemuth
Keyword(s):  
Heat Shock ◽  
Gene Family ◽  
Germ Line ◽  
Cell Lineage ◽  
Hsp70 Gene ◽  
Developmentally Regulated ◽  
Specific Expression ◽  
Hsp70 Mrna ◽  
Somatic Tissues ◽  
Exogenous Stress

Mouse somatic tissues contain low levels of transcripts homologous to the heat shock-inducible and cognate members of the heat shock protein 70 (hsp70) gene family. An abundant, unique sized hsp70 mRNA of 2.7 kilobases (kb) is present in testes in the absence of exogenous stress. Its expression is restricted to germ cells and is developmentally regulated. The 2.7-kb transcript first appears during the haploid phase of spermatogenesis and is stable throughout the morphogenic stages of spermiogenesis. A 2.7-kb hsp70 mRNA is present in rat and human testes. These observations suggest that a member of the hsp70 gene family plays a role in the development of the mammalian male germ cell lineage.

scholarly journals Identification of Genes Encoding CENP-A and Heterochromatin Protein 1 of Lipomyces starkeyi and Functional Analysis Using Schizosaccharomyces pombe

Genes ◽  
2020 ◽  
Vol 11 (7) ◽  
pp. 769
Author(s):  
Yuko Takayama
Keyword(s):  
Histone H3 ◽  
Specific Protein ◽  
Lipomyces Starkeyi ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Heterochromatin Formation ◽  
Histone H3 Variant ◽  
Genes Encoding ◽  
Almost All ◽  
Heterochromatin Structure

Centromeres function as a platform for the assembly of multiple kinetochore proteins and are essential for chromosome segregation. An active centromere is characterized by the presence of a centromere-specific histone H3 variant, CENP-A. Faithful centromeric localization of CENP-A is supported by heterochromatin in almost all eukaryotes; however, heterochromatin proteins have been lost in most Saccharomycotina. Here, identification of CENP-A (CENP-AL.s.) and heterochromatin protein 1 (Lsw1) in a Saccharomycotina species, the oleaginous yeast Lipomyces starkeyi, is reported. To determine if these proteins are functional, the proteins in S. pombe, a species widely used to study centromeres, were ectopically expressed. CENP-AL.s. localizes to centromeres and can be replaced with S. pombe CENP-A, indicating that CENP-AL.s. is a functional centromere-specific protein. Lsw1 binds at heterochromatin regions, and chromatin binding is dependent on methylation of histone H3 at lysine 9. In other species, self-interaction of heterochromatin protein 1 is thought to cause folding of chromatin, triggering transcription repression and heterochromatin formation. Consistent with this, it was found that Lsw1 can self-interact. L. starkeyi chromatin contains the methylation of histone H3 at lysine 9. These results indicated that L. starkeyi has a primitive heterochromatin structure and is an attractive model for analysis of centromere heterochromatin evolution.

scholarly journals Expression of a gene duplication encoding conserved sperm tail proteins is translationally regulated in Drosophila melanogaster.

1993 ◽  
Vol 13 (3) ◽  
pp. 1708-1718 ◽  
Author(s):  
M Schäfer ◽  
D Börsch ◽  
A Hülster ◽  
U Schäfer
Keyword(s):  
Drosophila Melanogaster ◽  
Gene Family ◽  
Translational Control ◽  
Germ Line ◽  
Gene Families ◽  
Homologous Gene ◽  
Male Sterile ◽  
Sperm Tail ◽  
Repetitive Motif ◽  
Carboxy Terminal

We have analyzed a locus of Drosophila melanogaster located at 98C on chromosome 3, which contains two tandemly arranged genes, named Mst98Ca and Mst98Cb. They are two additional members of the Mst(3)CGP gene family by three criteria. (i) Both genes are exclusively transcribed in the male germ line. (ii) Both transcripts encode a protein with a high proportion of the repetitive motif Cys-Gly-Pro. (iii) Their expression is translationally controlled; while transcripts can be detected in diploid stages of spermatogenesis, association with polysomes can be shown only in haploid stages of sperm development. The genes differ markedly from the other members of the gene family in structure; they do not contain introns, they are of much larger size, and they have the Cys-Gly-Pro motifs clustered at the carboxy-terminal end of the encoded proteins. An antibody generated against the Mst98Ca protein recognizes both Mst98C proteins in D. melanogaster. In a male-sterile mutation in which spermiogenesis is blocked before individualization of sperm, both of these proteins are no longer synthesized. This finding provides proof of late translation for the Mst98C proteins and thereby independent proof of translational control of expression. Northern (RNA) and Western immunoblot analyses indicate the presence of homologous gene families in many other Drosophila species. The Mst98C proteins share sequence homology with proteins of the outer dense fibers in mammalian spermatozoa and can be localized to the sperm tail by immunofluorescence with an anti-Mst98Ca antibody.

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