Wissmann AK et al. (1994) Worm Breeder's Gazette "Characterization of the let-502 Gene"

Mains PE, Wissmann AK, McGhee JD

[Worm Breeder's Gazette, 1994]

Characterization of the let-502 gene Andreas Wissmann, James D. McGhee and Paul E. Mains, Dept. of Medical Biochemistry, University of Calgary, Calgary, Alberta, Canada T2N 4N1

Stretton AOW et al. (1977) Worm Breeder's Gazette "neuroanatomy of Ascaris."

Donmoyer JE, Moses JER, Stretton AOW

[Worm Breeder's Gazette, 1977]

The motor nervous system of Ascaris consists of five sets of segmented neurons each containing eleven cells that make synapses onto muscle, together with six ventral interneurons that make synapses onto some of the motorneurons. The neurons can be divided into seven classes (see figure) that appear to be structurally identical to the seven classes in C. elegans, with the following equivalences . [See Figure 1] The dorsal n.m.j. cell types C, D and E receive interneuron input, but the A cell receives synapses only from ventral motorneurons. The ventral F and G cells receive input from interneurons; the B cells receive synapses only from dorsal motorneurons. All these output cells make synapses with muscle only in one nerve cord. Each segment has one copy of cell types A, D and E, and two copies of types B, C, F and G. Anatomical similarities (relative positions in nerve cords; details of the patterns of neuromuscular connectivity) are used to assign functional equivalences in the dorsal and ventral cords. [See Figure 2] The function of types of A, B, C, D and E neurons has been determined physiologically (see Walrond and Kass). The motorneuron synapses onto the inhibitory neurons provide pathways for reciprocal inhibition, between both cords, that is generated peripherally rather than centrally. [See Figure 3]

Hodgkin JA et al. (1993) Worm Breeder's Gazette "Caenorhabditis Genetic Map and Nomenclature E-Mailing List"

Hodgkin JA, O'Callaghan M

[Worm Breeder's Gazette, 1993]

Most of the points covered in the accompanying 'Nomenclature Guidelines -- New Recommendations' contribution were circulated by e-mail before the June 1993 meeting, to principal investigators with e-mail addresses, for their comments and reactions. This procedure appeared to be efficient and helpful. We wish to expand our e-mailing list for nomenclature issues, and for recommended methods of data submission. For this reason, we sent a message in August 1993 inviting other potentially interested parties to join this list, using the e-mail addresses from the 1993 WBG Subscriber Directory. We repeat this message below, for the benefit of readers who have e-mail access but did not receive our invitation. If you are interested, send us an e-mail message asking to be added to the list. From cgc@mrc-lmb.cam.ac.uk Dear WBG subscriber At present, CGC e-mail messages about methods of data submission, nomenclatorial issues and so on, are sent to all investigators with assigned lab codes (strain and allele designations) and known e-mail addresses. We would like to extend this mailing list to other interested parties who can be reached by e-mail. If you wish to be included on this expanded e-mailing list, please reply to this message, and you will be added to the list. Investigators already on the list need take no action. Regardless of whether you join the list, you will still be able to take note of any significant new recommendations, because these will be duly announced in issues of the Worm Yours sincerely, Jonathan Hodgkin Mary O'Callaghan

Otsuka AJ et al. (1991) Worm Breeder's Gazette "Comparison of the unc-104 Protein 'Motor' Domain with Members of the Kinesin Family of Proteins"

Tang LZ, Whiteaker K, Boontrakulpoontatwee P, Otsuka AJ, Zhang Y

[Worm Breeder's Gazette, 1991]

The unc-104 gene is capable of encoding a kinesin-related protein ( Otsuka et al., Neuron, in press). Comparison of the presumed unc-104 'motor' domain to the ATPase and microtubule-binding region of members of the kinesin family demonstrates the greatest sequence identity in the putative ATP-binding domain [GYN-TIFAYGQTGSGKTYTM-G] and in conserved elements of unknown function, some of which may be involved in microtubule-binding [GIIPR, VK-S(Y/F)-E(I/L)YNE, DLL, R-VA-T--N-- SSRSH-VF-I, SGKL-LVDLAGSE, GAEG-R--E--NINKSL--LG-VI-AL, HIPYR(D/E)SKLT- LLQ-SLGG, N--ET-STL-(F/Y)A-RAK--(R/K)]. In the figure below, residues that are identical in 5 or more sequences are listed below the compilation and asterisks mark residues that are identical in all sequences. [See Figure 1]

Sanford TR et al. (1982) Worm Breeder's Gazette "RNA polymerase from wild-type and alpha-amanitin-resistant C elegans."

Riddle DL, Sanford TR, Golomb M

[Worm Breeder's Gazette, 1982]

Partial purification of RNA polymerase II from C. elegans involves sonication of worms in high salt (ammonium sulfate), removal of nucleic acids by DEAE-cellulose chromatography in high salt, and separation of polymerases I and III from polymerase II on a DEAE- cellulose column eluted with a salt gradient. Polymerase assays utilize a calf thymus DNA template and are performed either in the presence or absence of amanitin. Pooled RNA polymerase II fractions from wild-type N2 and the EMS-induced amanitin-resistant mutant, DR432, were assayed with various concentrations of toxin to determine the degree of enzyme sensitivity in vitro. Polymerase II from DR432 (ama-1 IV) is approximately one hundred fold less sensitive to alpha- amanitin than is the wild-type enzyme. We tentatively conclude that ama-1 IV, closely linked to dpy-13, encodes a polymerase II subunit. RNA polymerase III has been partially resolved from polymerase I by DEAE-sephadex chromatography. A single chromatographic form of polymerase III elutes at 0.18M ammonium sulfate; its activity is stimulated approximately ten-fold by substituting poly-d(AT) for calf thymus DNA template. [See Figure 1] Amanitin sensitivity of RNA polymerase II from wild-type and amanitin-resistant C. elegans. Polymerase II isolated by DEAE-cellulose chromatography was assayed under standard conditions with varying amounts of amanitin. (Dark circles, wild-type; (open circles, enzyme from strain DR432(ama-1 IV).

Prasad BC et al. (1997) Worm Breeder's Gazette "unc-3 gene encodes the C elegans homologue of the mammalian transcription factor O/E-1"

Prasad BC, Reed RR

[Worm Breeder's Gazette, 1997]

The mammalian olfactory system utilizes specialized signal transduction components to detect odors. These olfactory genes contain consensus sites for a family of trans-acting factors which includes Olf-1/EBF (O/E-1). The O/E-1 protein is expressed at high level in adult olfactory neurons and transiently during embryogenesis in a variety of other neuronal tissues. The laboratory is actively trying to understand the role of this family of transcription factors in mouse neurodevelopment. We have identified a C elegans homologue of the mammalian O/E-1 protein. We believe that the C elegans homologue of O/E-1 (Ce O/E-1) is encoded by the unc-3 gene, mutations in which are reported to cause all classes of motor neurons in the ventral cord to have disorganized processes and make neuro-muscular junctions at ectopic sites. We have identified point mutations in the Ce O/E-1 coding region for three unc-3 alleles. We have used GFP fusions to the promoter of the Ce O/E-1 protein and specific antibodies to the protein to study the pattern of expression. The Ce O/E-1 protein is expressed as early as bean stage and continues to be expressed in the neurons of the ventral cord and the ASI chemosensory neurons throughout development. These observations are consistent with a similar role for O/E proteins in both mice and nematodes, i.e., these transcription factors play an essential role in the determination of the terminal phenotype of neurons.

Mains PE (1994) Worm Breeder's Gazette "Interactions Between mei-1 and the unc-116 Kinesin"

Mains PE

[Worm Breeder's Gazette, 1994]

Interactions Between mei-l and the unc-116 Kinesin Paul E. Mains, Dept. of Medical Biochemistry, University of Calgary, Calgary, Alberta, Canada

Kuwabara PE (1994) Worm Breeder's Gazette "Evidence For Interactions Between the Sex Determination and Dosage Compensation Pathways in the Germline"

Kuwabara PE

[Worm Breeder's Gazette, 1994]

Evidence for Interactions Between the Sex Determillation and Dosage Compensation Pathways in the Germline Patricia E. Kuwabara MRC-LMB Hills Road Cambridge CB2 2QH England

Musset-Bilal F et al. (1994) Worm Breeder's Gazette "Characterization of the C. elegans Basement Membrane-Associated Protein SPARC"

Musset-Bilal F, Schwarzbauer JE, Ryan CS

[Worm Breeder's Gazette, 1994]

Characterization of the C. elegans Basement Membrane- Associated Frederique Musset-Bilal, Carol S. Ryan, and Jean E. Schwarzbauer Department of Molecular Biology, Princeton University, Princeton NJ 08544

Goldstein B (1992) Worm Breeder's Gazette "Identification of the Cues Used to Generate Blastomere Diversity:The Role of the P2-EMS Interaction in Positioning Gut Fate Into E"

Goldstein B

[Worm Breeder's Gazette, 1992]

The gut of C. elegans derives from all the progeny of the E cell, a cell of the eight cell stage (Sulston et al. 1983 Dev. Biol. 100:64.) In order for E to form gut, EMS must contact P2 during the four cell stage (Goldstein 1992 Nature 357:255; [See Figure].) P2 'sposition on the "E" side of EMS raises the possibility that the P2 -EMSinteraction is the cue that makes E different from MS. Alternatively, the E and MS sides may be different from each other before the P2 -EMSinteraction, such that only the E side can form gut in response to the interaction. In order to determine which is the case, I tried to move P2 to the MS side of EMS, to see if MS then forms gut. This is a particularly frustrating manipulation. A more feasible way to address the question turned out to be isolating P2 and EMS, and then placing the two cells back in contact in a random orientation. If any side of EMS can form gut in response to the interaction, then gut should always form from the daughter of EMS that contacts P2 .If however only the E side can form gut, then in some cases either gut will form from the daughter away from P2 or gut will not differentiate. Fortunately, P2 and EMS stick immediately upon contact and they do not rotate around each other when placed back together, precluding the possibility that P2 moves back to its original position. Which daughter of EMS formed gut was then determined by one of two methods: In five cases cell division times were watched to see which daughter took on E-like cell division timings, and in another five cases the daughters of EMS were separated from each other and cultured individually to see which produced gut granules. Gut differentiated from the side of EMS on which P2 was placed in all ten cases. This result indicates that any side of EMS can form gut in response to the induction, and hence that the interaction with P2 is what makes E different from MS. Current work is aimed at identifying cellular mechanisms by which the induction makes E different than MS, and determining whether cell interactions are required at other stages for gut fate to be segregated into E.