Patricia J Walters et al. (2001) International C. elegans Meeting "Identification of lin-44(sa490ts) suppressors"

Patricia J Walters, Michael A Herman

[International C. elegans Meeting, 2001]

We are interested in genes involved in the control of cell polarity. We have focused on the postembryonic T blast cells in the tail whose polarities are controlled by lin-44 /Wnt. The goal of this research is to identify additional genes that function with lin-44 to control cell polarity. A proven genetic technique for identifying interacting genes in a genetic pathway is to isolate mutations that suppress or enhance a weak mutation affecting a gene in the pathway. This can often be achieved by using a conditional allele, such as a temperature sensitive (ts) allele, and adjusting the conditions such that only a weak defect is observed; for example, by placing a ts mutation at a temperature intermediate to the permissive and restrictive conditions. We have determined that lin-44(sa490) is temperature sensitive and have used this allele in genetic screens for lin-44(sa490ts) suppressors. To date, we have identified three suppressors. Preliminary genetic analysis indicates that all three suppressor mutations are extragenic. Currently, we are continuing our genetic analysis by mapping the suppressor mutations and pursuing efforts to identify new lin-44(sa490) suppressors.

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

Mehra A et al. (1994) Worm Breeder's Gazette "Direct Interaction Between FEM-3 and a Carboxy-Terminal Fragment of TRA-2A"

Spence AM, Heck L, Kuwabara PE, Mehra A

[Worm Breeder's Gazette, 1994]

Direct Interaction between FEM-3 and a Carboxy-Terminal Fragment Or TRA-2A Arun Mehra, Linda Heck, Patricia Kuwabara*, and Andrew Spence Dept. of Medical Genetics, University of Toronto, 1 King's College Circle, Toronto, Canada, and *MRC Laboratory of Molecular Biology, Hills Rd., Cambridge, UK

McGhee JD (1987) Biochemistry "Purification and characterization of a carboxylesterase from the intestine of the nematode Caenorhabditis elegans."

McGhee JD

[Biochemistry, 1987]

The major intestinal esterase from the nematode Caenorhabditis elegans has been purified to essential homogeneity. Starting from whole worms, the overall purification is 9000-fold with a 10% recovery of activity. The esterase is a single polypeptide chain of Mr 60,000 and is stoichiometrically inhibited by organophosphates. Substrate preferences and inhibition patterns classify the enzyme as a carboxylesterase (EC 3.1.1.1), but the physiological function is unknown. The sequence of 13 amino acid residues at the esterase N- terminus has been determined. This partial sequence shows a surprisingly high degree of similarity to the N-terminal sequence of two carboxylesterases recently isolated from Drosophila mojavensis [Pen, J., van Beeumen, J., & Beintema, J. J. (1986) Biochem. J. 238, 691-699].

Jon Pierce-Shimomura et al. (2002) Japanese Worm Meeting "Behavioral responses to ethanol are mediated by a BK potassium channel in C. elegans"

Antonello Bonci, Steve McIntire, Hongkyun Kim, Jon Pierce-Shimomura, Tod R Thiele, Andrew Davies

[Japanese Worm Meeting, 2002]

We screened for mutant C. elegans that are resistant to intoxication by ethanol. We found that strong resistance is conferred by mutations in the gene slo-1 , which encodes a highly conserved ortholog of the human large conductance calcium-activated potassium (BK) channel 1-3 . Prevous work has shown effects of ethanol on vertebrate BK channels in vitro 4-9 . We hypothesized that intoxication in C. elegans may be primarily mediated by ethanol activating the SLO-1 channel; thus strong resistance to intoxication by ethanol results when the SLO-1 channel is absent. To test this idea, we first performed in vivo whole-cell voltage-clamp recordings of dopamine neurons to identify a SLO-1 current that was present in neurons in wild-type worms but absent in slo-1 mutants. Next, we found that ethanol selectively and reversibly increased the amplitude of the outward-rectifying current in neurons of wild-type animals at physiologically relevant concentrations (20 & 100 mM). Ethanol had no effect, however, on currents in neurons of slo-1 mutants. To determine whether ethanol can activate SLO-1 directly in the absence of cytosolic factors, we recorded the single-channel activity of SLO-1 in patches excised from dopamine neurons. Ethanol reversibly increased the probability of channel opening. Thus, we have demonstrated a direct relationship between the SLO-1 channel, a biochemical effect of ethanol and a genetic effect on behavior 1 Wei et al (1996) Neuropharm; 2 Wang et al (2001) Neuron; 3 Chu et al (1998) Mol Pharmacol; 4 Dopico et al (1998) J Pharmacol Exp Ther; 5 Dopico et al (1996) Mol Pharmacol; 6 Dopico et al (1999) J Physiol; 7 Gruss et al (2001) Eur J Neurosci; 8 Jakab et al (1997) J Membr Biol; 9 Walters et al (2000) Am J Physiol Cell Physiol

Murakami S et al. (1999) Curr Biol "Life extension and stress resistance in Caenorhabditis elegans modulated by the tkr-1 gene."

Johnson TE, Murakami S

[Curr Biol, 1999]

In this Brief Communication, which appeared in the 14 September 1998 issue of Current Biology, the UV dose was reported erroneously. The dose reported was 20 J/m2 but the actual dose used was 0.4 J/cm2. Also, the gene formally referred to as tkr-1 has since been renamed old-1 (overexpression longevity determination).

Ramos CG et al. (2014) J Bacteriol "Retraction for Ramos et al., MtvR is a global small noncoding regulatory RNA in Burkholderia cenocepacia."

Feliciano JR, da Costa PJ, Ramos CG, Grilo AM, Leitao JH

[J Bacteriol, 2014]

Volume 195, no. 16, p. 35143523, 2013. A number of problems related to images published in this paper have been brought to our attention. Figure 1D contains duplicated images in lanes S and LE, and Fig. 4D and 6B contain images previously published in articles in this journal and in Microbiology and Microbial Pathogenesis, i.e., the following: C. G. Ramos, S. A. Sousa, A. M. Grilo, J. R. Feliciano, and J. H. Leitao, J. Bacteriol. 193:15151526, 2011. doi:10.1128/JB.01374-11. S. A. Sousa, C. G. Ramos, L. M. Moreira, and J. H. Leitao, Microbiology 156:896908, 2010. doi:10.1099/mic.0.035139-0. C. G. Ramos, S. A. Sousa, A. M. Grilo, L. Eberl, and J. H. Leitao, Microb. Pathog. 48:168177, 2010. doi: 10.1016/j.micpath.2010.02.006. Therefore, we retract the paper. We deeply regret this situation and apologize for any inconvenience to the editors and readers of Journal of Bacteriology, Microbial Pathogenesis, and Microbiology.

Nillegoda NB et al. (2015) Nature "Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation."

Berynskyy M, Morimoto RI, Bukau B, Stengel F, Kirstein J, Szlachcic A, Arnsburg K, Stank A, Scior A, Nillegoda NB, Gao X, Guilbride DL, Aebersold R, Wade RC, Mayer MP

[Nature, 2015]

Protein aggregates are the hallmark of stressed and ageing cells, and characterize several pathophysiological states. Healthy metazoan cells effectively eliminate intracellular protein aggregates, indicating that efficient disaggregation and/or degradation mechanisms exist. However, metazoans lack the key heat-shock protein disaggregase HSP100 of non-metazoan HSP70-dependent protein disaggregation systems, and the human HSP70 system alone, even with the crucial HSP110 nucleotide exchange factor, has poor disaggregation activity in vitro. This unresolved conundrum is central to protein quality control biology. Here we show that synergic cooperation between complexed J-protein co-chaperones of classes A and B unleashes highly efficient protein disaggregation activity in human and nematode HSP70 systems. Metazoan mixed-class J-protein complexes are transient, involve complementary charged regions conserved in the J-domains and carboxy-terminal domains of each J-protein class, and are flexible with respect to subunit composition. Complex formation allows J-proteins to initiate transient higher order chaperone structures involving HSP70 and interacting nucleotide exchange factors. A network of cooperative class A and B J-protein interactions therefore provides the metazoan HSP70 machinery with powerful, flexible, and finely regulatable disaggregase activity and a further level of regulation crucial for cellular protein quality control.

Miller DM et al. (1992) Worm Breeder's Gazette "unc-4 LacZ Expression in A-Type Motor Neurons"

Miller DM, Niemeyer CJ

[Worm Breeder's Gazette, 1992]

unc-4 LacZ expression in A-type motor neurons David M. Miller and Charles J. Niemeyer, Dept. of Cell Biology, Duke Univ. Medical Ctr, Durham, NC 27710

Sommer RJ et al. (1994) Worm Breeder's Gazette "Evolution of Vulva-Formation: Part II: Species With a Central Vulva"

Sommer RJ, Sternberg PW

[Worm Breeder's Gazette, 1994]

Evolution of vulva-formation: Part II: Species with a central vulva Ralf J. Sommer & Paul W. Sternberg, California Institute of Technology, Division of Biology 156-29, Pasadena, CA 91125