For a eukaryotic cell biologist, learning new things about old, familiar subjects (such as the differences between eukaryotes and prokaryotes) is one of the pleasures of teaching introductory biology courses. Such learning usually entails examining how bacteria function, in ways other than how they replicate and transcribe DNA and how they synthesize protein. It is interesting, for example, to understand how bacteria maintain their distinctive spherical, rod-like or spiral shapes; or how they make an external cell wall, if they have one; or how they segregate the products of DNA replication faithfully into daughter cells. New answers to these questions are especially interesting because, in this author's eukaryote-centric view, bacteria lack cytoskeletons and cytoskeletal proteins, which might be involved in maintaining cell shape, regulating cell wall synthesis, and erecting something like a mitotic apparatus. This introduces an equally delightful pleasure derived from teaching introductory biology: debunking worn-out notions. Bacteria do possess cytoskeletons made of proteins which resemble the actin and tubulin familiar to eukaryotic cell biologists. Here, the author reviews several recently-published videos that characterize the in vitro behaviors of the actin-like protein, ParM (also known as StbA), and the tubulin-like protein, FtsZ and its in situ localization during cell division. For sake of completeness, the author also briefly mentions some recent work on the protein crescentin (CreS), an intermediate filament-like molecule, in the absence of published videos. (Contains 4 figures and 1 footnote.)