Abstract
After lamins A, B and C were isolated and purified from rat liver, their assembly properties were examined by electron microscopy and scanning tunneling microscopy using negative staining and the glycerol coating method, respectively. By varying the assembly time or the ionic conditions under which polymerization takes place, we have observed different stages of lamin assembly, which may provide clues on the structure of the 10 nm lamin filaments. At the first level of structural organization, two lamin polypeptides associate laterally into dimers with the two domains being parallel and in register. At the second level of structural organization, two dimers associate in a half-staggered and antiparallel fashion to form a tetramer 75 nm in length. At the third level of structural organization, 4-10 lamin tetramers associate laterally in register to form 75 nm long 10nm filaments, which in turn combine head to head into long, fully assembled lamin filaments. The assembled lamin filaments are nonpolar.
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Min, G., Tong, X., Chen, B. et al. Assembly of lamins in vitro. Cell Res 6, 11–22 (1996). https://doi.org/10.1038/cr.1996.2
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DOI: https://doi.org/10.1038/cr.1996.2
