scholarly journals INDIRECT SUPPRESSION INVOLVING BEHAVIORAL MUTANTS WITH ALTERED NERVE EXCITABILITY IN DROSOPHILA MELANOGASTER

Genetics ◽  
1982 ◽  
Vol 100 (4) ◽  
pp. 597-614 ◽  
Author(s):  
Barry Ganetzky ◽  
Chun-Fang Wu
Keyword(s):  
Drosophila Melanogaster ◽  
Potential Temperature ◽  
Temperature Sensitive ◽  
Membrane Excitability ◽  
Nerve Activity ◽  
Functional Relationships ◽  
Nerve Excitability ◽  
Excitable Membranes ◽  
Allele Specific ◽  
And Function

ABSTRACT Two classes of X-linked behavioral mutants of Drosophila melanogaster, leg-shaking mutants and bang-sensitive mutants, are suppressed by napts (no action potential, temperature-sensitive), an autosomal temperature-sensitive paralytic mutation. So far, napts is found to suppress thirteen mutations at seven loci, two of which produce leg shaking and five bang-sensitivity. Suppression is recessive, occurs at temperatures permissive for napts, and is indirect and function-specific rather than allele-specific. At restrictive temperatures, napts is known to completely block all nerve activity. Several of the mutants suppressed by napts are shown by neurophysiological experiments to have increased nerve excitability. The physiological defect of these mutants as well as their behavioral defect is suppressed by napts. Thus, suppression occurs within individual neurons at the level of excitable membranes and apparently depends on the reduction in membrane excitability caused by napts even under permissive conditions. We suggest that all mutants suppressed by napts may have related defects leading to enhanced nerve excitability. Genetic interactions of this type help reveal functional relationships between different behavioral mutants and suggest ways of isolating new mutants with altered excitable membranes.

scholarly journals Analysis of TAF90 Mutants Displaying Allele-Specific and Broad Defects in Transcription

2001 ◽  
Vol 21 (21) ◽  
pp. 7331-7344 ◽  
Author(s):  
Robert J. Durso ◽  
Amy K. Fisher ◽  
Tiffany J. Albright-Frey ◽  
Joseph C. Reese
Keyword(s):  
Histone Acetyltransferase ◽  
Temperature Sensitive ◽  
Dramatic Reduction ◽  
Temperature Sensitive Mutants ◽  
General Transcription Factor ◽  
C Terminus ◽  
Number Of Genes ◽  
Allele Specific ◽  
And Function ◽  
Wd40 Repeats

ABSTRACT Yeast TAF90p is a component of at least two transcription regulatory complexes, the general transcription factor TFIID and the Spt-Ada-Gcn5 histone acetyltransferase complex (SAGA). Broad transcription defects have been observed in mutants of other TAFIIs shared by TFIID and SAGA but not in the only twoTAF90 mutants isolated to date. Given that the numbers of mutants analyzed thus far are small, we isolated and characterized 11 temperature-sensitive mutants of TAF90 and analyzed their effects on transcription and integrity of the TFIID and SAGA complexes. We found that the mutants displayed a variety of allele-specific defects in their ability to support transcription and maintain the structure of the TFIID and SAGA complexes. Sequencing of the alleles revealed that all have mutations corresponding to the C terminus of the protein, with most clustering within the conserved WD40 repeats; thus, the C terminus of TAF90p is required for its incorporation into TFIID and function in SAGA. Significantly, inactivation of one allele, taf90-20, caused the dramatic reduction in the levels of total mRNA and most specific transcripts analyzed. Analysis of the structure and/or activity of both TAF90p-containing complexes revealed that this allele is the most disruptive of all. Our analysis defines the requirement for the WD40 repeats in preserving TFIID and SAGA function, demonstrates that the defects associated with distinct mutations in TAF90 vary considerably, and indicates that TAF90 can be classified as a gene required for the transcription of a large number of genes.

scholarly journals BEHAVIORAL AND BIOCHEMICAL DEFECTS IN TEMPERATURE-SENSITIVE ACETYLCHOLINESTERASE MUTANTS OF DROSOPHILA MELANOGASTER

Genetics ◽  
1980 ◽  
Vol 96 (4) ◽  
pp. 939-965
Author(s):  
Jeffrey C Hall ◽  
Stamatis N Alahiotis ◽  
David A Strumpf ◽  
Kristin White
Keyword(s):  
Drosophila Melanogaster ◽  
Early Developmental Stage ◽  
Substrate Affinity ◽  
Temperature Sensitive ◽  
Restrictive Temperature ◽  
Permissive Temperature ◽  
Larval Stages ◽  
Cold Sensitive ◽  
And Function ◽  
Catalytic Functions

ABSTRACT Temperature-sensitive (ts) mutants of the Ace gene, which codes for acetylcholinesterase (AChE) in Drosophila melanogaster, were analyzed for defects in viability, behavior and function of the enzyme. The use of heat-sensitive and cold-sensitive mutations permited the function of AChE in the nervous system to be analyzed temporally. All ts mutations were lethal, or nearly so, when animals expressing them were subjected to restrictive temperatures during late embryonic and very early larval stages. Heat treatments to Ace-ts mid- and late larvae had little effect on the behavior of these animals or on the viability or behavior of the eventual adults. Heat-sensitive mutants exposed to nonpermissive temperatures as pupae, by contrast, had severe defects in phototaxis and locomotor activity as adults. AChE extracted from adult ts mutants that had developed at a permissive temperature were abnormally heat labile, and they had reduced substrate affinity when assayed at restrictive temperatures. However, enzyme activity did not decline during exposure of heat-sensitive adults to high temperatures even though such treatments caused decrements in phototaxis (29°) and, eventually, cessation of movement (31°). The cold-sensitive mutant also produced readily detectable levels of AChE when exposed to a restrictive temperature during the early developmental stage when this mutation causes almost complete lethality. We suggest that the relationship among the genetic, biochemical and neurobiological defects in these mutants may involve more than merely temperature-sensitive catalytic functions.

scholarly journals THE MECHANISM OF A BROODING EFFECT ASSOCIATED WITH SEGREGATION DISTORTION IN DROSOPHILA MELANOGASTER

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 619-631
Author(s):  
D L Hartl
Keyword(s):  
Drosophila Melanogaster ◽  
Segregation Distortion ◽  
Mature Sperm ◽  
Temperature Sensitive ◽  
Short Time

ABSTRACT The recovery of the SD chromosome from a heterozygous SD male increases with brood. This is independent of the age of the female, occurs during the time the sperm are stored in the females, disappears when the segregation distortion is suppressed, and is temperature-sensitive-temperature shocks above or below 25°C applied to the mature sperm both tend to accelerate the increase in the recovery of SD. All this suggests the existence of a class of sperm affected by SD in which the sperm are able to fertilize eggs for a short time following ejaculation but become dysfunctional thereafter.

A Family of Genes Clustered at the Triplo-lethal Locus of Drosophila melanogaster Has an Unusual Evolutionary History and Significant Synteny With Anopheles gambiae

Genetics ◽  
2003 ◽  
Vol 165 (2) ◽  
pp. 613-621 ◽  
Author(s):  
Douglas R Dorer ◽  
Jamie A Rudnick ◽  
Etsuko N Moriyama ◽  
Alan C Christensen
Keyword(s):  
Phylogenetic Analysis ◽  
Drosophila Melanogaster ◽  
Anopheles Gambiae ◽  
Evolutionary History ◽  
Codon Bias ◽  
Good Target ◽  
The Family ◽  
Genes Encoding ◽  
And Function ◽  
Gambiae Genome

Abstract Within the unique Triplo-lethal region (Tpl) of the Drosophila melanogaster genome we have found a cluster of 20 genes encoding a novel family of proteins. This family is also present in the Anopheles gambiae genome and displays remarkable synteny and sequence conservation with the Drosophila cluster. The family is also present in the sequenced genome of D. pseudoobscura, and homologs have been found in Aedes aegypti mosquitoes and in four other insect orders, but it is not present in the sequenced genome of any noninsect species. Phylogenetic analysis suggests that the cluster evolved prior to the divergence of Drosophila and Anopheles (250 MYA) and has been highly conserved since. The ratio of synonymous to nonsynonymous substitutions and the high codon bias suggest that there has been selection on this family both for expression level and function. We hypothesize that this gene family is Tpl, name it the Osiris family, and consider possible functions. We also predict that this family of proteins, due to the unique dosage sensitivity and the lack of homologs in noninsect species, would be a good target for genetic engineering or novel insecticides.

scholarly journals ADP-Ribosylation Factor (ARF) Interaction Is Not Sufficient for Yeast GGA Protein Function or Localization

2002 ◽  
Vol 13 (9) ◽  
pp. 3078-3095 ◽  
Author(s):  
Annette L. Boman ◽  
Paul D. Salo ◽  
Melissa J. Hauglund ◽  
Nicole L. Strand ◽  
Shelly J. Rensink ◽  
...  
Keyword(s):  
Membrane Trafficking ◽  
Mammalian Cells ◽  
Fluorescent Protein ◽  
Protein Localization ◽  
Carboxypeptidase Y ◽  
Minor Role ◽  
Temperature Sensitive ◽  
Adp Ribosylation ◽  
And Function ◽  
Adp Ribosylation Factor

Golgi-localized γ-ear homology domain, ADP-ribosylation factor (ARF)-binding proteins (GGAs) facilitate distinct steps of post-Golgi traffic. Human and yeast GGA proteins are only ∼25% identical, but all GGA proteins have four similar domains based on function and sequence homology. GGA proteins are most conserved in the region that interacts with ARF proteins. To analyze the role of ARF in GGA protein localization and function, we performed mutational analyses of both human and yeast GGAs. To our surprise, yeast and human GGAs differ in their requirement for ARF interaction. We describe a point mutation in both yeast and mammalian GGA proteins that eliminates binding to ARFs. In mammalian cells, this mutation disrupts the localization of human GGA proteins. Yeast Gga function was studied using an assay for carboxypeptidase Y missorting and synthetic temperature-sensitive lethality between GGAs andVPS27. Based on these assays, we conclude that non-Arf-binding yeast Gga mutants can function normally in membrane trafficking. Using green fluorescent protein-tagged Gga1p, we show that Arf interaction is not required for Gga localization to the Golgi. Truncation analysis of Gga1p and Gga2p suggests that the N-terminal VHS domain and C-terminal hinge and ear domains play significant roles in yeast Gga protein localization and function. Together, our data suggest that yeast Gga proteins function to assemble a protein complex at the late Golgi to initiate proper sorting and transport of specific cargo. Whereas mammalian GGAs must interact with ARF to localize to and function at the Golgi, interaction between yeast Ggas and Arf plays a minor role in Gga localization and function.

scholarly journals Spatio-temporal expression of Prospero is finely tuned to allow the correct development and function of the nervous system in Drosophila melanogaster

2007 ◽  
Vol 304 (1) ◽  
pp. 62-74 ◽  
Author(s):  
Laure Guenin ◽  
Yaël Grosjean ◽  
Stéphane Fraichard ◽  
Angel Acebes ◽  
Fawzia Baba-Aissa ◽  
...  
Keyword(s):  
Nervous System ◽  
Drosophila Melanogaster ◽  
Temporal Expression ◽  
Spatio Temporal ◽  
And Function

scholarly journals The trithorax Group Genemoira Encodes a Brahma-Associated Putative Chromatin-Remodeling Factor in Drosophila melanogaster

1999 ◽  
Vol 19 (2) ◽  
pp. 1159-1170 ◽  
Author(s):  
Madeline A. Crosby ◽  
Chaya Miller ◽  
, Tamar Alon ◽  
Kellie L. Watson ◽  
C. Peter Verrijzer ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Chromatin Remodeling ◽  
Leucine Zipper ◽  
Genetic Relationships ◽  
Fruit Fly ◽  
Protein Product ◽  
Homeotic Genes ◽  
Trithorax Group ◽  
Functional Relationships

ABSTRACT The genes of the trithorax group (trxG) inDrosophila melanogaster are required to maintain the pattern of homeotic gene expression that is established early in embryogenesis by the transient expression of the segmentation genes. The precise role of each of the diverse trxG members and the functional relationships among them are not well understood. Here, we report on the isolation of the trxG gene moira(mor) and its molecular characterization. morencodes a fruit fly homolog of the human and yeast chromatin-remodeling factors BAF170, BAF155, and SWI3. mor is widely expressed throughout development, and its 170-kDa protein product is present in many embryonic tissues. In vitro, MOR can bind to itself and it interacts with Brahma (BRM), an SWI2-SNF2 homolog, with which it is associated in embryonic nuclear extracts. The leucine zipper motif of MOR is likely to participate in self-oligomerization; the equally conserved SANT domain, for which no function is known, may be required for optimal binding to BRM. MOR thus joins BRM and Snf5-related 1 (SNR1), two known Drosophila SWI-SNF subunits that act as positive regulators of the homeotic genes. These observations provide a molecular explanation for the phenotypic and genetic relationships among several of the trxG genes by suggesting that they encode evolutionarily conserved components of a chromatin-remodeling complex.

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