Showing 211 - 220 of 257 Items
The role of behavioral diversity in determining the extent to which the cardiac ganglion is modulated in three species of crab
Date: 2020-01-01
Creator: Grace Bukowski-Thall
Access: Open access
- Central pattern generators (CPGs) are neural networks that generate the rhythmic outputs that control behaviors such as locomotion, respiration, and chewing. The stomatogastric nervous system (STNS), which contains the CPGs that control foregut movement, and the cardiac ganglion (CG), which is a CPG that controls heartbeat, are two commonly studied systems in decapod crustaceans. Neuromodulators are locally or hormonally released neuropeptides and amines that change the output patterns of CPGs like the STNS and CG to allow behavioral flexibility. We have hypothesized that neuromodulation provides a substrate for the evolution of behavioral flexibility, and as a result, systems exhibiting more behavioral flexibility are modulated to a greater degree. To examine this hypothesis, we evaluated the extent to which the STNS and the CG are modulated in the majoid crab species Chionoecetes opilio, Libinia emarginata, and Pugettia producta. C. opilio and L. emarginata are opportunistic feeders, whereas P. producta has a highly specialized kelp diet. We predicted that opportunistic feeding crabs that chew and process a wide variety of food types would exhibit greater STNS neuromodulatory capacity than those with a specialized diet. The STNS of L. emarginata and C. opilio responded to the seven endogenous neuromodulators oxotremorine, dopamine, CabTrp Ia, CCAP, myosuppressin, proctolin, and RPCH, whereas the STNS of P. producta only responded to proctolin, oxotremorine, myosuppressin, RPCH (25% of the time), variably to dopamine, and not at all to CabTrp and CCAP. Because P. producta, L. emarginata, and C. opilio all belong to the Majoidea superfamily, their primary distinctions are their feeding habits. For this reason, we further predicted that there would be no relationship between diet and modulatory capacity in the cardiac ganglion (CG) of the neurogenic heart. This would suggest that a lack of STNS modulatory capacity in P. producta relative to L. emarginata and C. opilio is specific to evolved foregut function. Whole-heart recordings from P. producta indicated that, unlike the STNS, the CG responds to CabTrp and CCAP. P. producta hearts also responded to oxotremorine and inconsistently to dopamine and proctolin. The CG of C. opilio was modulated by CabTrp, CCAP, dopamine, proctolin, myosuppressin, and oxotremorine, but not RPCH. The CG of L. emarginata responded to CCAP, and inconsistently to CabTrp, dopamine, and proctolin, but not to myosuppressin, RPCH, and surprisingly oxotremorine. Although cardiac responses were not identical between species, opportunistic and specialist feeders responded more similarly to the modulators tested in the heart than in the STNS. Notably, P. producta responded to each modulator in a similar manner to C. opilio and/or L. emarginata. However, L. emarginata’s surprising lack of cardiac response to oxotremorine suggests that phylogenetic closeness may not control for differences in CG and STNS function between species. Nevertheless, sample sizes of all three species were quite small, and individual differences lead to inconsistencies in the data. As a result, sample size must be enlarged to draw firm conclusions.
An Arabidopsis cell wall-associated kinase required for invertase activity and cell growth
Date: 2006-04-01
Creator: Bruce D. Kohorn, Masaru Kobayashi, Sue Johansen, Jeff Riese, Li Fen, Huang, Karen Koch, Sarita Fu, Anjali Dotson, Nicole Byers
Access: Open access
- The wall-associated kinases (WAK), a family of five proteins that contain extracellular domains that can be linked to pectin molecules of the cell wall, span the plasma membrane and have a cytoplasmic serine/threonine kinase domain. Previous work has shown that a reduction in WAK protein levels leads to a loss of cell expansion, indicating that these receptor-like proteins have a role in cell shape formation. Here it is shown that a single wak2 mutation exhibits a dependence on sugars and salts for seedling growth. This mutation also reduces the expression and activity of vacuolar invertase, often a key factor in turgor and expansion. WAKs may thus provide a molecular mechanism linking cell wall sensing (via pectin attachment) to regulation of solute metabolism, which in turn is known to be involved in turgor maintenance in growing cells. © 2006 The Authors.
The use of Hardy-Weinberg Equilibrium in clonal plant systems
Date: 2016-02-01
Creator: Vladimir Douhovnikoff, Matthew Leventhal
Access: Open access
- Traditionally population genetics precludes the use of the same genetic individual more than once in Hardy-Weinberg (HW) based calculations due to the model's explicit assumptions. However, when applied to clonal plant populations this can be difficult to do, and in some circumstances, it may be ecologically informative to use the ramet as the data unit. In fact, ecologists have varied the definition of the individual from a strict adherence to a single data point per genotype to a more inclusive approach of one data point per ramet. With the advent of molecular tools, the list of facultatively clonal plants and the recognition of their ecological relevance grows. There is an important risk of misinterpretation when HW calculations are applied to a clonal plant not recognized as clonal, as well as when the definition of the individual for those calculations is not clearly stated in a known clonal species. Focusing on heterozygosity values, we investigate cases that demonstrate the extreme range of potential modeling outcomes and describe the different contexts where a particular definition could better meet ecological modeling goals. We emphasize that the HW model can be ecologically relevant when applied to clonal plants, but caution is necessary in how it is used, reported, and interpreted. We propose that in known clonal plants, both genotype (GHet) and ramet (RHet) based calculations are reported to define the full range of potential values and better facilitate cross-study comparisons.
Does differential receptor distribution underlie variable responses to a neuropeptide in the lobster cardiac system?
Date: 2021-08-02
Creator: Audrey J. Muscato, Patrick Walsh, Sovannarath Pong, Alixander Pupo, Roni J., Gross, Andrew E. Christie, J. Joe Hull, Patsy S. Dickinson
Access: Open access
- Central pattern generators produce rhythmic behaviors independently of sensory input; however, their outputs can be modulated by neuropeptides, thereby allowing for functional flexibility. We investigated the effects of C-type allatostatins (AST-C) on the cardiac ganglion (CG), which is the central pattern generator that controls the heart of the American lobster, Homarus americanus, to identify the biological mechanism underlying the significant variability in individual responses to AST-C. We proposed that the presence of multiple receptors, and thus differential receptor distribution, was at least partly responsible for this observed variability. Using transcriptome mining and PCR-based cloning, we identified four AST-C receptors (ASTCRs) in the CG; we then characterized their cellular localization, binding potential, and functional activation. Only two of the four receptors, ASTCR1 and ASTCR2, were fully functional GPCRs that targeted to the cell surface and were activated by AST-C peptides in our insect cell expression system. All four, however, were amplified from CG cDNAs. Following the confirmation of ASTCR expression, we used physiological and bioinformatic techniques to correlate receptor expression with cardiac responses to AST-C across individuals. Expression of ASTCR1 in the CG showed a negative correlation with increasing contraction amplitude in response to AST-C perfusion through the lobster heart, suggesting that the differential expression of ASTCRs within the CG is partly responsible for the specific physiological response to AST-C exhibited by a given individual lobster.
Assessment and comparison of putative amine receptor complement/diversity in the brain and eyestalk ganglia of the lobster, Homarus americanus
Date: 2020-06-01
Creator: Andrew E. Christie, J. Joe Hull, Patsy S. Dickinson
Access: Open access
- In decapods, dopamine, octopamine, serotonin, and histamine function as locally released/hormonally delivered modulators of physiology/behavior. Although the functional roles played by amines in decapods have been examined extensively, little is known about the identity/diversity of their amine receptors. Recently, a Homarus americanus mixed nervous system transcriptome was used to identify putative neuronal amine receptors in this species. While many receptors were identified, some were fragmentary, and no evidence of splice/other variants was found. Here, the previously predicted proteins were used to search brain- and eyestalk ganglia-specific transcriptomes to assess/compare amine receptor complements in these portions of the lobster nervous system. All previously identified receptors were reidentified from the brain and/or eyestalk ganglia transcriptomes, i.e., dopamine alpha-1, beta-1, and alpha-2 (Homam-DAα2R) receptors, octopamine alpha (Homam-OctαR), beta-1, beta-2, beta-3, beta-4, and octopamine–tyramine (Homam-OTR-I) receptors, serotonin type-1A, type-1B (Homam-5HTR1B), type-2B, and type-7 receptors; and histamine type-1 (Homam-HA1R), type-2, type-3, and type-4 receptors. For many previously partial proteins, full-length receptors were deduced from brain and/or eyestalk ganglia transcripts, i.e., Homam-DAα2R, Homam-OctαR, Homam-OTR-I, and Homam-5HTR1B. In addition, novel dopamine/ecdysteroid, octopamine alpha-2, and OTR receptors were discovered, the latter, Homam-OTR-II, being a putative paralog of Homam-OTR-I. Finally, evidence for splice/other variants was found for many receptors, including evidence for some being assembly-specific, e.g., a brain-specific Homam-OTR-I variant and an eyestalk ganglia-specific Homam-HA1R variant. To increase confidence in the transcriptome-derived sequences, a subset of receptors was cloned using RT-PCR. These data complement/augment those reported previously, providing a more complete picture of amine receptor complement/diversity in the lobster nervous system.
Examining Functional Roles for Anthocyanins in Plant Leaves Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2016-05-01
Creator: Benjamin M West
Access: Access restricted to the Bowdoin Community
Three Decades of Replicated Field Studies Reveal Eelgrass (Zostera marina) Inhibits Soft-shell Clam (Mya arenaria) Growth in Eastern Maine This record is embargoed.
- Embargo End Date: 2027-05-16
Date: 2024-01-01
Creator: Everett Horch
Access: Embargoed
Functional redundancy of a non-native foundation species (eelgrass, Zostera japonica) across intertidal stress gradients
Date: 2023-01-01
Creator: S. Maria Garcia
Access: Open access
- Non-native species foundation species can alter ecosystems in both positive and negative ways. The creation of habitat can be beneficial to native species when they provide a limiting resource or in a stressful environment. Yet this creation of habitat can also be detrimental by replacing native species and/or facilitating the presence of more non-native species. In Willapa Bay, WA, a non-native foundation species, Zostera japonica, co-exists with the native foundation species Zostera marina. Zostera japonica persists at the higher intertidal in monocultures, the two species overlap in the mid intertidal, and Z. marina persists in monocultures in the low intertidal. Epifaunal invertebrates, the organisms that live on eelgrass blades, connect eelgrass to higher trophic levels. Through a series of transplants and removals, I used this zonation pattern to ask if the two species can fulfill a similar functional role in respect to epifaunal invertebrates (functional redundancy), and if this was due to the identity of the foundation species or a response to the stress gradient of the intertidal. My results suggest that the epifaunal invertebrate community is responding more to the physiological stress gradient, and the functional redundancy of the two species depends on the location they are found. Z. japonica is expanding the range of vegetated habitat into to the physiologically stressful high zone, which supports a different community. This experiment highlights that the impacts of non- native species are highly localized and that abiotic and biotic factors are important to trophic interactions.
Identification of methylated proteins in the yeast small ribosomal subunit: A role for SPOUT methyltransferases in protein arginine methylation
Date: 2012-06-26
Creator: Brian D. Young, David I. Weiss, Cecilia I. Zurita-Lopez, Kristofor J. Webb, Steven G., Clarke, Anne E. McBride
Access: Open access
- We have characterized the posttranslational methylation of Rps2, Rps3, and Rps27a, three small ribosomal subunit proteins in the yeast Saccharomyces cerevisiae, using mass spectrometry and amino acid analysis. We found that Rps2 is substoichiometrically modified at arginine-10 by the Rmt1 methyltransferase. We demonstrated that Rps3 is stoichiometrically modified by ω- monomethylation at arginine-146 by mass spectrometric and site-directed mutagenic analyses. Substitution of alanine for arginine at position 146 is associated with slow cell growth, suggesting that the amino acid identity at this site may influence ribosomal function and/or biogenesis. Analysis of the three-dimensional structure of Rps3 in S. cerevisiae shows that arginine-146 makes contacts with the small subunit rRNA. Screening of deletion mutants encoding potential yeast methyltransferases revealed that the loss of the YOR021C gene results in the absence of methylation of Rps3. We demonstrated that recombinant Yor021c catalyzes ω-monomethylarginine formation when incubated with S-adenosylmethionine and hypomethylated ribosomes prepared from a YOR021C deletion strain. Interestingly, Yor021c belongs to the family of SPOUT methyltransferases that, to date, have only been shown to modify RNA substrates. Our findings suggest a wider role for SPOUT methyltransferases in nature. Finally, we have demonstrated the presence of a stoichiometrically methylated cysteine residue at position 39 of Rps27a in a zinc-cysteine cluster. The discovery of these three novel sites of protein modification within the small ribosomal subunit will now allow for an analysis of their functional roles in translation and possibly other cellular processes. © 2012 American Chemical Society.
Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function
Date: 2009-08-05
Creator: Anne E. McBride, Ana K. Conboy, Shanique P. Brown, Chaiyaboot Ariyachet, Kate L., Rutledge
Access: Open access
- The discovery of roles for arginine methylation in intracellular transport and mRNA splicing has focused attention on the methylated arginine-glycine (RG)-rich domains found in many eukaryotic RNA-binding proteins. Sequence similarity among these highly repetitive RG domains, combined with interactions between RG-rich proteins, raises the question of whether these regions are general interaction motifs or whether there is specificity within these domains. Using the essential Saccharomyces cerevisiae mRNA-binding protein Npl3 (ScNpl3) as a model system, we first tested the importance of the RG domain for protein function. While Npl3 lacking the RG domain could not support growth of cells lacking Npl3, surprisingly, expression of the RG domain alone supported partial growth of these cells. To address the specificity of this domain, we created chimeric forms of ScNpl3 with RG-rich domains of S. cerevisiae nucleolar proteins, Gar1 and Nop1 (ScGar1, ScNop1), or of the Candida albicans Npl3 ortholog (CaNpl3). Whereas the CaNpl3 RG chimeric protein retained nearly wild-type function in S. cerevisiae, the ScGar1 and ScNop1 RG domains significantly reduced Npl3 function and self-association, indicating RG domain specificity. Nuclear localization of Npl3 also requires specific RG sequences, yet heterologous RG domains allow similar modulation of Npl3 transport by arginine methylation.