Gene_locus Report for: dicdi-crysp

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Amoebozoa: N E > Mycetozoa: N E > Dictyosteliida: N E > Dictyostelium: N E > Dictyostelium discoideum: N E

Title: The genome of the social amoeba Dictyostelium discoideum
Eichinger L, Pachebat JA, Glockner G, Rajandream MA, Sucgang R, Berriman M, Song J, Olsen R, Szafranski K and Kuspa A <87 more author(s)> Eichinger L, Pachebat JA, Glockner G, Rajandream MA, Sucgang R, Berriman M, Song J, Olsen R, Szafranski K, Xu Q, Tunggal B, Kummerfeld S, Madera M, Konfortov BA, Rivero F, Bankier AT, Lehmann R, Hamlin N, Davies R, Gaudet P, Fey P, Pilcher K, Chen G, Saunders D, Sodergren E, Davis P, Kerhornou A, Nie X, Hall N, Anjard C, Hemphill L, Bason N, Farbrother P, Desany B, Just E, Morio T, Rost R, Churcher C, Cooper J, Haydock S, van Driessche N, Cronin A, Goodhead I, Muzny D, Mourier T, Pain A, Lu M, Harper D, Lindsay R, Hauser H, James K, Quiles M, Madan Babu M, Saito T, Buchrieser C, Wardroper A, Felder M, Thangavelu M, Johnson D, Knights A, Loulseged H, Mungall K, Oliver K, Price C, Quail MA, Urushihara H, Hernandez J, Rabbinowitsch E, Steffen D, Sanders M, Ma J, Kohara Y, Sharp S, Simmonds M, Spiegler S, Tivey A, Sugano S, White B, Walker D, Woodward J, Winckler T, Tanaka Y, Shaulsky G, Schleicher M, Weinstock G, Rosenthal A, Cox EC, Chisholm RL, Gibbs R, Loomis WF, Platzer M, Kay RR, Williams J, Dear PH, Noegel AA, Barrell B, Kuspa A (- 87)
Ref: Nature, 435:43, 2005 : PubMed
Abstract


ESTHER: Eichinger_2005_Nature_435_43
PubMedSearch: Eichinger 2005 Nature 435 43
PubMedID: 15875012
Gene_locus related to this paper: dicdi-abhd, dicdi-ACHE, dicdi-apra, dicdi-cinbp, dicdi-CMBL, dicdi-crysp, dicdi-DPOA, dicdi-P90528, dicdi-ppme1, dicdi-Q8MYE7, dicdi-q54cf7, dicdi-q54cl7, dicdi-q54cm0, dicdi-q54ct5, dicdi-q54cu1, dicdi-q54d54, dicdi-q54d66, dicdi-q54dj5, dicdi-q54dy7, dicdi-q54ek1, dicdi-q54eq6, dicdi-q54et1, dicdi-q54et7, dicdi-q54f01, dicdi-q54g24, dicdi-q54g47, dicdi-q54gi7, dicdi-q54gw5, dicdi-q54gx3, dicdi-q54h23, dicdi-q54h73, dicdi-q54i38, dicdi-q54ie5, dicdi-q54in4, dicdi-q54kz1, dicdi-q54l36, dicdi-q54li1, dicdi-q54m29, dicdi-q54n21, dicdi-q54n35, dicdi-q54n85, dicdi-q54qe7, dicdi-q54qi3, dicdi-q54qk2, dicdi-q54rl3, dicdi-q54rl8, dicdi-q54sy6, dicdi-q54sz3, dicdi-q54t49, dicdi-q54t91, dicdi-q54th2, dicdi-q54u01, dicdi-q54vc2, dicdi-q54vw1, dicdi-q54xe3, dicdi-q54xl3, dicdi-q54xu1, dicdi-q54xu2, dicdi-q54y48, dicdi-q54yd0, dicdi-q54ye0, dicdi-q54yl1, dicdi-q54yr8, dicdi-q54z90, dicdi-q55bx3, dicdi-q55d01, dicdi-q55d81, dicdi-q55du6, dicdi-q55eu1, dicdi-q55eu8, dicdi-q55fk4, dicdi-q55gk7, dicdi-Q54ZA6, dicdi-q86h82, dicdi-Q86HC9, dicdi-Q86HM5, dicdi-Q86HM6, dicdi-q86iz7, dicdi-q86jb6, dicdi-Q86KU7, dicdi-q550s3, dicdi-q552c0, dicdi-q553t5, dicdi-q555e5, dicdi-q555h0, dicdi-q555h1, dicdi-q557k5, dicdi-q558u2, dicdi-Q869Q8, dicdi-u554, dicdi-y9086, dicdi-q54r44, dicdi-f172a

Abstract

The social amoebae are exceptional in their ability to alternate between unicellular and multicellular forms. Here we describe the genome of the best-studied member of this group, Dictyostelium discoideum. The gene-dense chromosomes of this organism encode approximately 12,500 predicted proteins, a high proportion of which have long, repetitive amino acid tracts. There are many genes for polyketide synthases and ABC transporters, suggesting an extensive secondary metabolism for producing and exporting small molecules. The genome is rich in complex repeats, one class of which is clustered and may serve as centromeres. Partial copies of the extrachromosomal ribosomal DNA (rDNA) element are found at the ends of each chromosome, suggesting a novel telomere structure and the use of a common mechanism to maintain both the rDNA and chromosomal termini. A proteome-based phylogeny shows that the amoebozoa diverged from the animal-fungal lineage after the plant-animal split, but Dictyostelium seems to have retained more of the diversity of the ancestral genome than have plants, animals or fungi.



        

Title: Membrane-enclosed crystals in Dictyostelium discoideum cells, consisting of developmentally regulated proteins with sequence similarities to known esterases
Bomblies L, Biegelmann E, Doring V, Gerisch G, Krafft-Czepa H, Noegel AA, Schleicher M, Humbel BM
Ref: Journal of Cell Biology, 110:669, 1990 : PubMed
Abstract


ESTHER: Bomblies_1990_J.Cell.Biol_110_669
PubMedSearch: Bomblies 1990 J.Cell.Biol 110 669
PubMedID: 2307702
Gene_locus related to this paper: dicdi-crd2p, dicdi-crysp, dicdi-drgen

Abstract

Developing cells of Dictyostelium discoideum contain crystalline inclusion bodies. The interlattice spaces of the crystals are approximately 11 nm, and their edge dimensions vary in aggregating cells from 0.1 to 0.5 micron. The crystals are enclosed by a membrane with the characteristics of RER. To unravel the nature of the crystals we isolated them under electron microscopical control and purified the two major proteins that cofractionate with the crystals, one of an apparent molecular mass of 69 kD, the other of 56 kD. This latter protein proved to be identical with the protein encoded by the developmentally regulated D2 gene of D. discoideum, as shown by its reactivity with antibodies raised against the bacterially expressed product of a D2 fusion gene. The D2 gene is known to be strictly regulated at the transcript level and to be controlled by cAMP signals. Accordingly, very little of the 56-kD protein was detected in growth phase cells, maximal expression was observed at the aggregation stage, and the expression was stimulated by cAMP pulses. The 69-kD protein is the major constituent of the crystals and is therefore called "crystal protein." This protein is developmentally regulated and accumulates in aggregating cells similar to the D2 protein, but is not, or is only slightly regulated by cAMP pulses. mAbs specific for either the crystal protein or the D2 protein, labeled the intracellular crystals as demonstrated by the use of immunoelectron microscopy. The complete cDNA-derived amino acid sequence of the crystal protein indicates a hydrophobic leader and shows a high degree of sequence similarity with Torpedo acetylcholinesterase and rat lysophospholipase. Because the D2 protein also shows sequence similarities with various esterases, the vesicles filled with crystals of these proteins are named esterosomes.