Knock-down gene Ubiquitin Carboxy-Terminal Hydrolase (duch) resulted in reducing tyrosine hydroxylase in dopaminergic cells and inducing apoptosis in Drosophila melanogaster

2015 ◽  
Vol 37 (1se) ◽  
Author(s):  
Dang Ngoc Anh Suong ◽  
Tran Hoang Hiep ◽  
Nguyen Thi Thanh ◽  
Dang Thi Phuong Thao
Keyword(s):  
Drosophila Melanogaster ◽  
Tyrosine Hydroxylase ◽  
Dopaminergic Cells ◽  
Knock Down ◽  
Carboxy Terminal

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.

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.

scholarly journals A fragmented alignment method detects a putative phosphorylation site and a putative BRC repeat in the Drosophila melanogaster BRCA2 protein

F1000Research ◽  
2013 ◽  
Vol 2 ◽  
pp. 143
Author(s):  
Sandeep Chakraborty
Keyword(s):  
Drosophila Melanogaster ◽  
Phosphorylation Site ◽  
Tumor Suppressor Protein ◽  
Alignment Method ◽  
Checkpoint Kinases ◽  
Link Type ◽  
Putative Phosphorylation Site ◽  
Brca2 Protein ◽  
Integral Role ◽  
Carboxy Terminal

Mutations in the BRCA2 tumor suppressor protein leave individuals susceptible to breast, ovarian and other cancers. The BRCA2 protein is a critical component of the DNA repair pathways in eukaryotes, and also plays an integral role in fostering genomic variability through meiotic recombination. Although present in many eukaryotes, as a whole the BRCA2 gene is weakly conserved. Conserved fragments of 30 amino acids (BRC repeats), which mediate interactions with the recombinase RAD51, helped detect orthologs of this protein in other organisms. The carboxy-terminal of the human BRCA2 has been shown to be phosphorylated by checkpoint kinases (Chk1/Chk2) at T3387, which regulate the sequestration of RAD51 on DNA damage. However, apart from three BRC repeats, the Drosophila melanogaster gene has not been annotated and associated with other functionally relevant sequence fragments in human BRCA2. In the current work, the carboxy-terminal phosphorylation threonine site (E=9.1e-4) and a new BRC repeat (E=17e-4) in D. melanogaster has been identified, using a fragmented alignment methodology (FRAGAL). In a similar study, FRAGAL has also identified a novel half-a- tetratricopeptide (HAT) motif (E=11e-4), a helical repeat motif implicated in various aspects of RNA metabolism, in Utp6 from yeast. The characteristic three aromatic residues with conserved spacing are observed in this new HAT repeat, further strengthening my claim. The reference and target sequences are sliced into overlapping fragments of equal parameterized lengths. All pairs of fragments in the reference and target proteins are aligned, and the gap penalties are adjusted to discourage gaps in the middle of the alignment. The results of the best matches are sorted based on differing criteria to aid the detection of known and putative sequences. The source code for FRAGAL results on these sequences is available at https://github.com/sanchak/FragalCode, while the database can be accessed at www.sanchak.com/fragal.html.

Thimerosal inhibits Drosophila melanogaster tyrosine hydroxylase (DmTyrH) leading to changes in dopamine levels and impaired motor behavior: implications for neurotoxicity

Metallomics ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 362-374 ◽  
Author(s):  
Matheus C. Bianchini ◽  
Claudia Ortiz Alves Gularte ◽  
Pablo A. Nogara ◽  
Bárbara N. Krum ◽  
Mateus C. Gayer ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Tyrosine Hydroxylase ◽  
Motor Behavior ◽  
Antiseptic Agent

Thimerosal (THIM) is a well-established antifungal and antiseptic agent widely used as a preservative in vaccines.

scholarly journals Odd-skipped controls neurite morphology and affect cell survival in Drosophila Melanogaster CNS

2020 ◽  
Author(s):  
Yeoh Sue Lynn ◽  
Alina Letzel ◽  
Clemence Bernard Hannah Somerfield ◽  
Kyle Kyser ◽  
Emily Lin ◽  
...  
Keyword(s):  
Cell Death ◽  
Transcription Factor ◽  
Drosophila Melanogaster ◽  
Synapse Formation ◽  
Neurite Growth ◽  
Neural Function ◽  
Induce Cell Death ◽  
Over Expression ◽  
Knock Down ◽  
Protein Levels

AbstractThe transcription factor Odd-skipped has been implicated in many developmental processes in Drosophila melanogaster. Odd-skipped is expressed in a small cluster of neurons (Slater, Levy et al.) in the developing and adult CNS but its role in neurogenesis has so far not been addressed. Here we show that Odd-skipped plays a pivotal role in neurite growth and arborization during development. Loss-of-Odd-skipped function prevents neurite outgrowth whereas over and miss-expression causes neurite growth and arborization defects. In addition, miss-expression of Odd-skipped can induce cell death in some neural sub types. The neurite growth and arborization defects associated with Odd-skipped over expression correlates with a reduction in the pre-synaptically targeted protein Bruchpilot in axonal arbours suggesting an overall decrease in Odd neural synapse formation. This is supported by behavioural data showing that larvae in which Odd-skipped is overexpressed behave similarly to larvae in which Odd neurons are silenced showing that increasing Odd-skipped protein levels affect neural function. Finally, we demonstrate that using RNAi against Odd-skipped does not knock down Odd-skipped protein but instead cause an increase in protein levels compared to control larvae. This data demonstrates that RNAi can cause up-regulation of protein levels highlighting the importance of verifying protein levels when using RNAi approaches for knock-down.

Sign in / Sign up

Export Citation Format

Share Document