GENETIC LOCALIZATION AND BIOCHEMICAL CHARACTERIZATION OF A TRANS-ACTING REGULATORY EFFECT IN DROSOPHILA

ABSTRACT A region-specific, trans-acting regulatory gene that alters in vivo protein levels of α-glycerophosphate dehydrogenase (α-GPDH) has been mapped to position 55.4 on the third chromosome of Drosophila melanogaster. The gene has been found to affect the in vivo stability of α-GPDH in adult thoracic tissue but has no effect on α-GPDH levels in the abdomen. Although no other thoracic proteins were found to be influenced by the locus, it appears to modify the level of one additional abdominal protein. The action of the gene over development and its possible mode of control are discussed.

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Post-Translational Control of Alcohol Dehydrogenase Levels in Drosophila melanogaster

Genetics ◽

10.1093/genetics/115.4.693 ◽

1987 ◽

Vol 115 (4) ◽

pp. 693-699

Author(s):

Joseph J King ◽

John F McDonald

Keyword(s):

Drosophila Melanogaster ◽

Alcohol Dehydrogenase ◽

Translational Control ◽

Total Protein ◽

Regulatory Gene ◽

Protein Levels ◽

The Third

ABSTRACT A trans-acting regulatory gene that alters in vivo protein levels of alcohol dehydrogenase (ADH) has been mapped to a region of the third chromosome of Drosophila melanogaster. The gene has been found to affect the in vivo stability of ADH protein. It was not found to alter levels of total protein of two other enzymes assayed. The action of the gene over development and its possible mode of control are discussed.

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Biochemical Characterization of the Drosophila Wingless Signaling Pathway Based on RNA Interference

Molecular and Cellular Biology ◽

10.1128/mcb.24.5.2012-2024.2004 ◽

2004 ◽

Vol 24 (5) ◽

pp. 2012-2024 ◽

Cited By ~ 35

Author(s):

Hiroko Matsubayashi ◽

Sonoka Sese ◽

Jong-Seo Lee ◽

Tadaoki Shirakawa ◽

Takeshi Iwatsubo ◽

...

Keyword(s):

Rna Interference ◽

Biochemical Characterization ◽

The Other ◽

Protein Levels ◽

Culture Cells ◽

Tissue Culture Cells ◽

Mediated Priming ◽

Kinase A

ABSTRACT Regulation of Armadillo (Arm) protein levels through ubiquitin-mediated degradation plays a central role in the Wingless (Wg) signaling. Although zeste-white3 (Zw3)-mediated Arm phosphorylation has been implicated in its degradation, we have recently shown that casein kinase Iα (CKIα) also phosphorylates Arm and induces its degradation. However, it remains unclear how CKIα and Zw3, as well as other components of the Arm degradation complex, regulate Arm phosphorylation in response to Wg. In particular, whether Wg signaling suppresses CKIα- or Zw3-mediated Arm phosphorylaytion in vivo is unknown. To clarify these issues, we performed a series of RNA interference (RNAi)-based analyses in Drosophila S2R+ cells by using antibodies that specifically recognize Arm phosphorylated at different serine residues. These analyses revealed that Arm phosphorylation at serine-56 and at threonine-52, serine-48, and serine-44, is mediated by CKIα and Zw3, respectively, and that Zw3-directed Arm phosphorylation requires CKIα-mediated priming phosphorylation. Daxin stimulates Zw3- but not CKIα-mediated Arm phosphorylation. Wg suppresses Zw3- but not CKIα-mediated Arm phosphorylation, indicating that a vital regulatory step in Wg signaling is Zw3-mediated Arm phosphorylation. In addition, further RNAi-based analyses of the other aspects of the Wg pathway clarified that Wg-induced Dishevelled phosphoylation is due to CKIα and that presenilin and protein kinase A play little part in the regulation of Arm protein levels in Drosophila tissue culture cells.

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Synthesis, Quantification, and Characterization of Fatty Acid Amides from In Vitro and In Vivo Sources

Molecules ◽

10.3390/molecules26092543 ◽

2021 ◽

Vol 26 (9) ◽

pp. 2543

Author(s):

Ruidong Ni ◽

Suzeeta Bhandari ◽

Perry R. Mitchell ◽

Gabriela Suarez ◽

Neel B. Patel ◽

...

Keyword(s):

Drosophila Melanogaster ◽

Fatty Acid ◽

Apis Mellifera ◽

Chemical Synthesis ◽

Acid Amide ◽

Fatty Acid Amides ◽

Fatty Acid Amide

Fatty acid amides are a diverse family of underappreciated, biologically occurring lipids. Herein, the methods for the chemical synthesis and subsequent characterization of specific members of the fatty acid amide family are described. The synthetically prepared fatty acid amides and those obtained commercially are used as standards for the characterization and quantification of the fatty acid amides produced by biological systems, a fatty acid amidome. The fatty acid amidomes from mouse N18TG2 cells, sheep choroid plexus cells, Drosophila melanogaster, Bombyx mori, Apis mellifera, and Tribolium castaneum are presented.

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Biochemical characterization of Yin Yang 1 – RNA complexes

Biochemistry and Cell Biology ◽

10.1139/o07-155 ◽

2008 ◽

Vol 86 (1) ◽

pp. 31-36 ◽

Cited By ~ 12

Author(s):

Zachery R. Belak ◽

Andrew Ficzycz ◽

Nick Ovsenek

Keyword(s):

Rna Binding ◽

Biochemical Characterization ◽

Ribonucleoprotein Complexes ◽

Yin Yang 1 ◽

Significant Difference ◽

Yin Yang ◽

Rna Interaction ◽

Rna Complexes

YY1 (Yin Yang 1) is present in the Xenopus oocyte cytoplasm as a constituent of messenger ribonucleoprotein complexes (mRNPs). Association of YY1 with mRNPs requires direct RNA-binding activity. Previously, we have shown YY1 has a high affinity for U-rich RNA; however, potential interactions with plausible in vivo targets have not been investigated. Here we report a biochemical characterization of the YY1–RNA interaction including an investigation of the stability, potential 5′-methylguanosine affinity, and specificity for target RNAs. The formation of YY1–RNA complexes in vitro was highly resistant to thermal, ionic, and detergent disruption. The endogenous oocyte YY1–mRNA interactions were also found to be highly stable. Specific YY1–RNA interactions were observed with selected mRNA and 5S RNA probes. The affinity of YY1 for these substrates was within an order of magnitude of that for its cognate DNA element. Experiments aimed at determining the potential role of the 7-methylguanosine cap on RNA-binding reveal no significant difference in the affinity of YY1 for capped or uncapped mRNA. Taken together, the results show that the YY1–RNA interaction is highly stable, and that YY1 possesses the ability to interact with structurally divergent RNA substrates. These data are the first to specifically document the interaction between YY1 and potential in vivo targets.

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Isolation and characterization of the dopa decarboxylase gene of Drosophila melanogaster

Molecular and Cellular Biology ◽

10.1128/mcb.1.6.475-485.1981 ◽

1981 ◽

Vol 1 (6) ◽

pp. 475-485

Author(s):

J Hirsh ◽

N Davidson

Keyword(s):

Drosophila Melanogaster ◽

Ribonucleic Acid ◽

Deoxyribonucleic Acid ◽

Isolation Procedure ◽

Chromosome Band ◽

Dopa Decarboxylase ◽

Developmental Profile ◽

Isolation And Characterization

We have isolated chromosomal deoxyribonucleic acid clones containing the Drosophila dopa decarboxylase gene. We describe an isolation procedure which can be applied to other nonabundantly expressed Drosophila genes. The dopa decarboxylase gene lies within or very near polytene chromosome band 37C1-2. The gene is interrupted by at least one intron, and the primary mode of regulation is pretranslational. At least two additional sequences hybridized by in vivo ribonucleic acid-derived probes are found within a 35-kilobase region surrounding the gene. The developmental profile of ribonucleic acid transcribed from one of these regions differs from that of the dopa decarboxylase transcript.

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