A Transparent Window into Biology: A Primer on Caenorhabditis elegans.
Bottom Line: We survey the basic anatomical features, common technical approaches, and important discoveries in C. elegans research.Key to studying C. elegans has been the ability to address biological problems genetically, using both forward and reverse genetics, both at the level of the entire organism and at the level of the single, identified cell.These possibilities make C. elegans useful not only in research laboratories, but also in the classroom where it can be used to excite students who actually can see what is happening inside live cells and tissues.
Affiliation: Biology Department, The Catholic University of America, Washington, DC 20064 firstname.lastname@example.org email@example.com firstname.lastname@example.org.Show MeSH
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Mentions: C. elegans is a tiny, free-living nematode found worldwide. Newly hatched larvae are 0.25 mm long and adults are 1 mm long. Their small size means that the animals usually are observed with either dissecting microscopes, which generally allow up to 100X magnification, or compound microscopes, which allow up to 1000X magnification. The dissecting microscope is used to observe worms on Petri dishes (Figure 1, A and B) as they move, eat, develop, mate, and lay eggs (for movies showing these features, see http://labs.bio.unc.edu/Goldstein/movies.html). A compound or confocal microscope allows observation at much finer resolution (Figure 1C), permitting researchers to perform experiments that address questions related to cell development and function at single-cell resolution. Because C. elegans is transparent, individual cells and subcellular details are easily visualized using Nomarski (differential interference contrast, DIC) optics (Figure 1C). Enhanced detail can be discerned by using fluorescent proteins to tag proteins or subcellular compartments (Figure 1D). Fluorescent proteins can also be used to study developmental processes, screen for mutants affecting cell development and function, isolate cells, and characterize protein interactions in vivo (Chalfie et al. 1994; Boulin et al. 2006; Feinberg et al. 2008).
Affiliation: Biology Department, The Catholic University of America, Washington, DC 20064 email@example.com firstname.lastname@example.org email@example.com.