Disease relevance of Cry

• The Cry family of Bacillus thuringiensis insecticidal and nematicidal proteins constitutes a valuable source of environmentally benign compounds for the control of insect pests and disease agents [1].

High impact information on Cry

• By DNA sequencing of gene 1, the homology was localized within the same two regions already conserved between the small hsp genes: a central region of 83 amino acids, homologous with the mammalian alpha crystallin and the first 15 N-terminal amino acids [2].
• We show a strong interaction between Veela and cryptochrome genetic variants, demonstrating that the Jetlag, Timeless, and Cry proteins function in the same pathway [3].
• The use of model invertebrates, such as Caenorhabditis elegans and Drosophila melanogaster, as well as advances in insect genomics, are likely to accelerate efforts to clone Cry toxin resistance genes and come to a detailed and broad understanding of Cry toxin resistance [1].
• Despite unexpected heterogeneity and diversity in their DNA sequences, many studies have revealed that most of the Crystallin genes are regulated by a relatively small set of developmentally important transcription factors [4].
• The results show that the DC5 enhancer is not only active in the compound eye but, remarkably, is specifically active in those cells responsible for Crystallin secretion in Drosophila, i.e. the cone cells [4].

Biological context of Cry

• Resistance to Cry toxins has uncovered a four component glycosylation pathway that is functionally conserved between nematodes and insects and that provides the basis of the dominant mechanism of resistance in C. elegans [5].
• During lens fiber cell differentiation, the regulation of crystallin gene expression is coupled with dramatic morphological changes [6].
• Cubomedusan jellyfish have three novel crystallin families (the J-crystallins); the J1-crystallins are encoded in three very similar intronless genes with markedly different 5' flanking sequences despite their almost identical encoded proteins and high lens expression [7].
• PaxB binds to and activates Tripedalia crystallin promoters (especially J3-crystallin) and the Drosophila rhodopsin rh6 gene in transfection tests and induces ectopic eyes in Drosophila [8].

Anatomical context of Cry

• In Drosophila melanogaster, the circadian clock is synchronized with the natural environment by light-dependent degradation of the clock protein Timeless, mediated by the blue-light photoreceptor Cryptochrome (Cry) [3].
• The eye lens contains a structural protein, alpha crystallin, composed of two homologous primary gene products alpha A2 and alpha B2 [9].
• Drosocrystallin is one of three calcium binding taxon-specific crystallins found selectively in the acellular corneal lens of Drosophila, while antigen 3G6 is a highly conserved protein present in the ommatidial crystallin cone and central nervous system of numerous arthropods [7].
• alpha-Crystallin protein cognates were found in germ cells of the Indianmeal moth, Plodia interpunctella (Shirk and Zimowska, 1997) [10].
• alpha-Crystallin protein cognates in eggs of the moth, Plodia interpunctella: possible chaperones for the follicular epithelium yolk protein [10].

Associations of Cry with chemical compounds

• Drosocrystallin, a major 52 kDa glycoprotein of the Drosophila melanogaster corneal lens. Purification, biochemical characterization, and subcellular localization [11].

Other interactions of Cry

• We now have identified and characterized a candidate blue light photoreceptor gene in Drosophila (DCry) that is homologous to the cryptochrome (Cry) genes of mammals and plants [12].
• Like Pax6, PaxB activates jellyfish crystallin and Drosophila rhodopsin rh6 promoters and induces small ectopic eyes in Drosophila [13].

Analytical, diagnostic and therapeutic context of Cry

• In situ hybridization showed that PaxB and crystallin genes are expressed in the lens, retina and statocysts [8].

References