Drosophila proteins

Nuclear factor kappa B (NF-kB) is the generic term for a family of dimeric eukaryotic transcription factors, composed of members of the Rel family of DNA-binding proteins including the mammalian proteins RelA (or p65), cRel, RelB, p50 and p52, and the Drosophila proteins Dorsal, Dif and Relish. These proteins bind with different affinities to a consensus DNA sequence motif (called the kB site) consisting of the sequence 5 -GGGRNNYYCC-3 in which R is a purine, Y is a pyrimidine, and N is any base. 

The Rel homology domain (RHD) is an evolutionarily conserved domain found in some eukaryotic transcription factors, including NF-kB, the nuclear factors of activated T-cells (NFATs) and the drosophila proteins Dif and Relish. Some of these transcription factors form... 

Bray, S. J., Burke, B., Brown, N. H., and Hirsh, J. (1989). Embryonic expression pattern of a family of Drosophila proteins which interact with a CNS regulatory element. Genes Dev. 3 1130-1145. 

Kerrebrock AW, Moore DP, Wu JS, Orr-Weaver TL 1995 Mei-S332, a Drosophila protein required for sister-chromatid cohesion, can localize to meiotic centromere regions. Cell 83 247-256... 

Vucic, D., W. J. Kaiser, and L. K. Miller, Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by Drosophila proteins HID and GRIM. Mol Cell Biol, 1998, 18(6), 3300-9. 

Bennet, E. J., Bjerregaard, J., Knapp, J. E., Chavous, D. A., Friedman, A. M., Royer, W. E., and O Connor, C. M. (2003). Catalytic implications from the Drosophila protein L-isoaspartyl methyltransferase structure and site-directed mutagenesis. Biochemistry 42, 12844-12853. 

Park, S.K., Mann, K. J., Lin, H., Starostina, E., Kolski-Andreaco, A. and Pikielny, C. W. (2006). A Drosophila protein specific to pheromone-sensing gustatory hairs delays males copulation attempts. Curr. Biol., 16, 1154-1159. 

Starostina, E Xu, A., Lin, H. and Pikienly, C. W. (2008). A Drosophila protein family implicated in pheromone perception is related to Tay-Sachs GM2-activator protein.. /. Biol. Chem., 284, 585-594. 

A large protein family that contains extracellular domains homologous to EGF is called the EGF-domain proteins. EGF-like domains or modules are often found in many extracellular and membrane proteins (>70). They are involved in blood coagulation, fibrinolysis and the complement systems, matrix proteins, cell surface receptors, the low-density hpoprotein receptor and the developmentally important receptor. Notch. EGF-like domains may exist as multiple copies within proteins such as in the Drosophila protein Notch with 36 copies or as a single copy as in EGF itself It can also be found in conjunction with other modules. 

SMAD Proteins homologs of both the drosophila protein, mothers against decapentaplegic (MAD) and the C. 

The proteoglycans in this family, which includes decorin, biglycan, lumican, and fibromodulin, are major components of the interstitial matrix produced by fibroblasts and other cells. The core proteins are small (37-45 kDa) and have several leucine-rich motifs [112] with similarity to the LH-CG receptor, thyrotropin receptor, and Drosophila proteins chaoptin and toll. Core proteins of this family characteristically undergo proteolytic processing following synthesis, with removal of an additional small peptide from the N-terminus. 

Fig. 4.8 Protein family/disease ortholog view of the Drosophila protein-interaction map. Proteins are color-coded according to protein family as annotated by the Gene Ontology hierarchy. Proteins orthologous to human disease proteins have a jagged, starry border. Interactions were sorted ac-...

Toll signaling now appears to be one of the most evolu-tionarily conserved processes known. All the components between Toll and the activation of Dorsal have been largely conserved. There are 8 Drosophila proteins related to Toll plus Toll itself and 10 Toll-related human proteins that control the production of a wide variety of antimicrobial peptides in flies and cytokines in mammals. These molecules provide a rapid, nonspecific defense against infection by a wide array of pathogens. The adaptive immune response mounted by vertebrates, involving antibodies and T cells, is directed against specific pathogens but is slower to develop than the innate, nonspecific response. 

EXAMPLE 6.19 SoS is a protein that is involved in signaling pathways that are initiated by growth factor receptors (see Sec. 6.7). It derives its name from a protein called Sevenless, which (when present in mutant form) leads to defects in the development of the fruit fly Drosophila. Proteins with sequence similarity to Sevenless were subsequently discovered in mammals. One of them was called Son of Sevenless, abbreviated as SoS. (Yes, molecular cell biologists do have a sense of humor )... 

Kussel, P., and Frasch, M. (1995a). Pendulin, a Drosophila protein with cell cycle-dependent nuclear localization, is required for normal cell proliferation. J. Cell Biol. 129, 1491-1507. 

Methylation of histone lysine residues is catalysed by site- and methylation-state specific i.e. tri-/di-/monomethylation states) histone methyltransferases (EC number 2.1.1.43, Table 5.4). With the exception of DOTIL, which methylates H3K79, all identified KMTs catalyse methylation using a SET domain (SET is an abbreviation for Su(var)3-9, Enhancer of zeste and Trithorax and refers to the Drosophila protein suppressor of variegation where this domain was first identified). ... 

L., Cherbas, P., Kaufinann, T. C., Miller, D. F., Mechref, Y., Novotny, M. V, Ewing, M. A., Sporleder C. R., Clemmer, D. E. (2003) Development of high-sensitivity ion trap ion mobility spectrometry time-of-flight techniques a high-throughput nano-LC-IMS-TOF separation of peptides arising from a Drosophila protein extract. Anal Chem, 75, 5137-5145. 

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