Dear Leung Kim,

We purchase our DIF-1 from Enzo Life Sciences.
Kind regards,

Sascha.


Am 25.03.2011 15:05 Uhr schrieb "Leung Kim" unter <[log in to unmask]>:

> Hi,
> 
> I would like to know which vendor sells DIF-1 nowadays. Thanks in advance.
> 
> Best,
> Leung Kim
> Associate Professor
> Florida International University
> Miami, Fl USA 33199
>  
> On Mar 4, 2011, at 5:27 PM, dictyBase wrote:
> 
>> dictyNews
>> Electronic Edition
>> Volume 36, number 7
>> March 4, 2011
>> 
>> Please submit abstracts of your papers as soon as they have been
>> accepted for publication by sending them to [log in to unmask]
>> or by using the form at
>> http://dictybase.org/db/cgi-bin/dictyBase/abstract_submit.
>> 
>> Back issues of dictyNews, the Dicty Reference database and other
>> useful information is available at dictyBase - http://dictybase.org.
>> 
>> Follow dictyBase on twitter:
>> http://twitter.com/dictybase
>> 
>> 
>> =========
>> Abstracts
>> =========
>> 
>> Comparative genomics of the social amoebae Dictyostelium discoideum
>> and Dictyostelium purpureum
>> 
>> Richard Sucgang1*, Alan Kuo2*, Xiangjun Tian3*, William Salerno1*, Anup
>> Parikh4, 
>> Christa L. Feasley5, Eileen Dalin2, Hank Tu2, Eryong Huang4, Kerrie Barry2,
>> Erika Lindquist2, Harris Shapiro2, David Bruce2, Jeremy Schmutz2, Asaf
>> Salamov2, 
>> Petra Fey6, Pascale Gaudet6, Christophe Anjard7, M. Madan Babu8, Siddhartha
>> Basu6, 
>> Yulia Bushmanova6, Hanke van der Wel5, Mariko Katoh-Kurasawa4, Christopher
>> Dinh1, 
>> Pedro M. Coutinho9, Tamao Saito10, Marek Elias11, Pauline Schaap12, Robert R.
>> Kay8, 
>> Bernard Henrissat9, Ludwig Eichinger13, Francisco Rivero14, Nicholas H.
>> Putnam3, 
>> Christopher M. West5, William F. Loomis7, Rex L. Chisholm6, Gad Shaulsky3,4,
>> Joan E. Strassmann3, David C. Queller3, Adam Kuspa1,3,4,†, and Igor V.
>> Grigoriev2
>> 
>> 1Verna and Marrs McLean Department of Biochemistry and Molecular Biology,
>> Baylor 
>> College of Medicine, Houston, TX 77030
>> 2U.S. Department of Energy Joint Genome Institute, Walnut Creek CA
>> 3Department of Ecology and Evolutionary Biology, Rice University, Houston, TX
>> 77005; 
>> 4Department of Molecular and Human Genetics, Baylor College of Medicine,
>> Houston, 
>> TX 77030 
>> 5Department of Biochemistry & Molecular Biology, Oklahoma Center for Medical
>> Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City,
>> OK 73104
>> 6dictyBase, Center for Genetic Medicine, Northwestern University, 750 N Lake
>> Shore 
>> Drive, Chicago, Illinois 60611
>> 7Section of Cell and Developmental Biology, Division of Biology, University
>> of California, 
>> San Diego, La Jolla, California 92093
>> 8Laboratory of Molecular Biology, MRC Centre, Cambridge CB2 2QH, UK
>> 9Architecture et Fonction des Macromolécules Biologiques, UMR6098, CNRS,
>> Universities of Aix-Marseille I & II, 13288 Marseille, France
>> 10Department of Materials and Life Sciences, Sophia University 7-1 Kioi-Cho,
>> Chiyoda-Ku, Tokyo, Japan 102-8554
>> 11Departments of Botany and Parasitology, Faculty of Science, Charles
>> University 
>> in Prague, Prague, Czech Republic
>> 12College of Life Sciences, University of Dundee, DD15EH Dundee, UK
>> 13Center for Molecular Medicine Cologne, University of Cologne,
>> Joseph-Stelzmann-Str.
>> 52, 50931 Cologne, Germany
>> 14Centre for Biomedical Research, The Hull York Medical School and Department
>> of 
>> Biological Sciences, University of Hull, Hull HU6 7RX, UK.
>> 
>> 
>> Genome Biology, in press
>> 
>> Background:
>> The social amoebae (Dictyostelia) are a diverse group of Amoebozoa that
>> achieve 
>> multicellularity by aggregation and undergo morphogenesis into fruiting
>> bodies with 
>> terminally differentiated spores and stalk cells. There are four groups of
>> dictyostelids, 
>> with the most derived being a group that contains the model species
>> Dictyostelium 
>> discoideum. 
>> Results: 
>> We have produced a draft genome sequence of another group Dictyostelid,
>> Dictyostelium 
>> purpureum, and compare it to the D. discoideum genome. The assembly (8.41x
>> coverage) 
>> comprises 799 scaffolds totaling 33.0 Mb, comparable to the D. discoideum
>> genome size. 
>> Sequence comparisons suggest that these two Dictyostelids shared a common
>> ancestor 
>> approximately 400 million years ago. In spite of this divergence, most
>> orthologs reside in
>> small clusters of conserved synteny. Comparative analyses revealed a core set
>> of 
>> orthologous genes that illuminate Dictyostelid physiology, as well as
>> differences in gene
>> family content. Interesting patterns of gene conservation and divergence are
>> also evident 
>> suggesting function differences; some protein families, such as the histidine
>> kinases, 
>> have undergone little functional change, whereas others, such as the
>> polyketide synthases,
>> have undergone extensive diversification. The abundant amino acid
>> homopolymers 
>> encoded in both genomes are generally not found in homologous positions
>> within proteins,
>> so they are unlikely to derive from ancestral DNA triplet repeats. Genes
>> involved in the 
>> social stage evolved more rapidly than others, consistent with either relaxed
>> selection 
>> or accelerated evolution due to social conflict.
>> Conclusion:
>> The findings from this new genome sequence and comparative analysis shed
>> light on 
>> the biology and evolution of the Dictyostelia.
>> 
>> 
>> Submitted by Adam Kuspa [[log in to unmask]]
>> -----------------------------------------------------------------------------
>> ---
>> 
>> 
>> Deficiency of huntingtin has pleiotropic effects in the social amoeba
>> Dictyostelium discoideum
>> 
>> Michael A. Myre1, Amanda L. Lumsden1, Morgan N. Thompson1,
>> Wilma Wasco2, Marcy E. MacDonald1 and James F. Gusella1
>> 
>> 1Molecular Neurogenetics Unit, Center for Human Genetic Research,
>> Massachusetts General Hospital, Boston MA 02114.
>> 
>> 2Genetics and Aging Research Unit, MassGeneral Institute for
>> Neurodegenerative
>> Disease, Massachusetts General Hospital, Charlestown MA 02129.
>> 
>> PLoS Genetics, in press
>> 
>> Huntingtin is a large HEAT repeat protein first identified in humans, where a
>> polyglutamine 
>> tract expansion near the amino terminus causes a gain-of-function mechanism
>> that leads 
>> to selective neuronal loss in Huntington’s disease (HD). Genetic evidence in
>> humans and 
>> knock-in mouse models suggests that this gain-of-function involves an
>> increase or 
>> deregulation of some aspect of huntingtin’s normal function(s), which remains
>> poorly 
>> understood. As huntingtin shows evolutionary conservation, a powerful
>> approach to 
>> discovering its normal biochemical role(s) is to study the effects caused by
>> its deficiency 
>> in a model organism with a short life-cycle that comprises both cellular and
>> multicellular 
>> developmental stages. To facilitate studies aimed at detailed knowledge of
>> huntingtin’s 
>> normal function(s), we generated a null mutant of hd, the HD ortholog in
>> Dictyostelium 
>> discoideum. Dictyostelium cells lacking endogenous huntingtin were viable but
>> during 
>> development did not exhibit the typical polarized morphology of Dictyostelium
>> cells, 
>> streamed poorly to form aggregates by accretion rather than chemotaxis,
>> showed 
>> disorganized F-actin staining, exhibited extreme sensitivity to hypoosmotic
>> stress, 
>> and failed to form EDTA-resistant cell-cell contacts. Surprisingly,
>> chemotactic 
>> streaming could be rescued in the presence of the bivalent cations Ca2+ or
>> Mg2+ 
>> but not pulses of cAMP. Although hd- cells completed development, it was
>> delayed 
>> and proceeded asynchronously, producing small fruiting bodies with round,
>> defective 
>> spores that germinated spontaneously within a glassy sorus. When developed as
>> chimeras with wild-type cells, hd- cells failed to populate the pre-spore
>> region of the 
>> slug. In Dictyostelium, huntingtin deficiency is compatible with survival of
>> the organism 
>> but renders cells sensitive to low osmolarity which produces pleiotropic cell
>> autonomous 
>> defects that affect cAMP signaling, and as a consequence development. Thus,
>> Dictyostelium provides a novel haploid organism model for genetic, cell
>> biological 
>> and biochemical studies to delineate the functions of the HD protein.
>> 
>> 
>> 
>> Submitted by Michael Myre [[log in to unmask]]
>> -----------------------------------------------------------------------------
>> ---
>> 
>> A Dictyostelium SH2 adaptor protein required for correct DIF-1 signaling and
>> pattern formation
>> 
>> 
>> Christopher Sugden1, Susan Ross1, Sarah J. Annesley4, Christian Cole1,
>> Gareth Bloomfield3, Alasdair Ivens2 Jason Skelton2, Paul R. Fisher4,
>> Geoffrey Barton1 and Jeffrey G. Williams1*
>> 
>> 1School of Life Sciences, University of Dundee, Dow St., Dundee, DD1 5EH UK
>> 2Wellcome Trust Sanger Institute, Hinxton, CB10 1SA UK
>> 3MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH UK
>> 4Department of Microbiology, La Trobe University, Bundoora, Victoria 3086,
>> Australia
>> * Corresponding Author
>> [log in to unmask]
>> tel 44 1382 385220,
>> fax 44-1382 34421
>> 
>> 
>> Dev. Biol., in press
>> 
>> Dictyostelium is the only non-metazoan with functionally analysed SH2 domains
>> and studying them can give insights into their evolution and wider potential.
>> LrrB 
>> has a novel domain configuration with leucine-rich repeat, 14-3-3 and SH2
>> protein-protein interaction modules. It is required for the correct
>> expression of 
>> several specific genes in early development and here we characterize its role
>> in 
>> later, multicellular development. During development in the light, slug
>> formation 
>> in LrrB null (lrrB-) mutants is delayed relative to the parental strain, and
>> the slugs 
>> are highly defective in phototaxis and thermotaxis. In the dark the mutant
>> arrests 
>> development as an elongated mound, in a hitherto unreported process we term
>> dark stalling. The developmental and phototaxis defects are cell autonomous
>> and 
>> marker analysis shows that the pstO prestalk sub-region of the slug is
>> aberrant in 
>> the lrrB- mutant. Expression profiling, by parallel micro-array and deep RNA
>> sequence analyses, reveals many other alterations in prestalk-specific gene
>> expression in lrrB- slugs, including reduced expression of the ecmB gene and
>> elevated expression of ampA. During culmination ampA is ectopically expressed
>> in the stalk, there is no expression of ampA and ecmB in the lower cup and
>> the 
>> mutant fruiting bodies lack a basal disc. The basal disc cup derives from the
>> pstB 
>> cells and this population is greatly reduced in the lrrB- mutant. This
>> anatomical 
>> feature is a hallmark of mutants aberrant in signalling by DIF-1, the
>> polyketide 
>> that induces prestalk and stalk cell differentiation. In a DIF-1 induction
>> assay 
>> the lrrB- mutant is profoundly defective in ecmB activation but only
>> marginally 
>> defective in ecmA induction. Thus the mutation partially uncouples these two
>> inductive events. In early development LrrB interacts physically and
>> functionally 
>> with CldA, another SH2 domain containing protein. However, the CldA null
>> mutant does not phenocopy the lrrB- in its aberrant multicellular development
>> or phototaxis defect, implying that the early and late functions of LrrB are
>> effected in different ways. These observations, coupled with its domain
>> structure, suggest that LrrB is an SH2 adaptor protein active in diverse
>> developmental signaling pathways.
>> 
>> 
>> Submitted by: Jeff Williams [[log in to unmask]]
>> ==============================================================
>> [End dictyNews, volume 36, number 7]

-- 
Dr. Sascha Thewes
Institut für Biologie - Mikrobiologie
Fachbereich Biologie, Chemie, Pharmazie
Freie Universität Berlin
Königin-Luise-Str. 12-16
D-14195 Berlin

Tel.: 030-838-53373
Fax: 030-838-57773
Email: [log in to unmask]
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